Phosphoinositides in Control of Membrane Dynamics

Schink, Kay O.; Tan, Kia-Wee; Stenmark, Harald

doi:10.1146/annurev-cellbio-111315-125349

Cited by 284Cellular transport and secretionProtein Kinase Regulation and GTPase SignalingLipid Membrane Structure and Behavior

The DOI matches its Crossref record; 157 of the 158 references it cites were found in a registry or an index.

Phosphoinositides in Control of Membrane Dynamics

Schink, Kay O., Tan, Kia-Wee, Stenmark, Harald·2016·Annual Review of Cell and Developmental Biology

DOI 10.1146/annurev-cellbio-111315-125349

Open this paper in CoChat — free account

Abstract

Most functions of eukaryotic cells are controlled by cellular membranes, which are not static entities but undergo frequent budding, fission, fusion, and sculpting reactions collectively referred to as membrane dynamics. Consequently, regulation of membrane dynamics is crucial for cellular functions. A key mechanism in such regulation is the reversible recruitment of cytosolic proteins or protein complexes to specific membranes at specific time points. To a large extent this recruitment is orchestrated by phosphorylated derivatives of the membrane lipid phosphatidylinositol, known as phosphoinositides. The seven phosphoinositides found in nature localize to distinct membrane domains and recruit distinct effectors, thereby contributing strongly to the maintenance of membrane identity. Many of the phosphoinositide effectors are proteins that control membrane dynamics, and in this review we discuss the functions of phosphoinositides in membrane dynamics during exocytosis, endocytosis, autophagy, cell division, cell migration, and epithelial cell polarity, with emphasis on protein effectors that are recruited by specific phosphoinositides during these processes.

Integrity signals

Registry

Crossref · 10.1146/annurev-cellbio-111315-125349

Cites

157 of 157 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

PI(4,5)P2 is a substrate for PLC and PI3K.
“PI(4,5)P2 is a substrate for two signalling pathways.”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [10]
PLC hydrolysis of PI(4,5)P2 generates IP3 and DAG.
“Phospholipase C (PLC) leads to the generation of two second messengers, inositol(1,4,5)trisphosphate (I(1,4,5)P3), known trigger for mobilising Ca2+ from endoplasmic reticulum (ER) stores and diacylglycerol (DAG), an activator for protein kinase C (PKC).”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [10]
IP3 mobilises Ca2+ from ER stores.
“Phospholipase C (PLC) leads to the generation of two second messengers, inositol(1,4,5)trisphosphate (I(1,4,5)P3), known trigger for mobilising Ca2+ from endoplasmic reticulum (ER) stores and diacylglycerol (DAG), an activator for protein kinase C (PKC).”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [10]
DAG activates PKC.
“Phospholipase C (PLC) leads to the generation of two second messengers, inositol(1,4,5)trisphosphate (I(1,4,5)P3), known trigger for mobilising Ca2+ from endoplasmic reticulum (ER) stores and diacylglycerol (DAG), an activator for protein kinase C (PKC).”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [10]
PI3K generates PI(3,4,5)P3, a lipid with wide-ranging functions.
“The second pathway is phosphoinositide-3-kinase (PI3K) to make PI(3,4,5)P3, a lipid with wide-ranging functions.”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [10]

Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452
Regulated portals of entry into the cell
Conner, S. D., & Schmid, S. L. (2003) · Nature · doi:10.1038/nature01451 · Cited by 3,959
Rab GTPases as coordinators of vesicle traffic
Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413
Self-citation
Phosphoinositides in cell regulation and membrane dynamics
Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790
Molecular mechanism and physiological functions of clathrin-mediated endocytosis
McMahon, H. T., & Boucrot, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3151 · Cited by 2,223
Membrane Fusion: Grappling with SNARE and SM Proteins
Südhof, T. C., & Rothman, J. E. (2009) · Science · doi:10.1126/science.1161748 · Cited by 2,027
Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
Axe, E. L., Walker, S. A., Manifava, M., Chandra, P., Roderick, H. L., Habermann, A., Griffiths, G., & Ktistakis, N. T. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200803137 · Cited by 1,885
GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors
Rossman, K. L., Der, C. J., & Sondek, J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1587 · Cited by 1,697
Autophagosomes form at ER–mitochondria contact sites
Hamasaki, M., Furuta, N., Matsuda, A., Nezu, A., Yamamoto, A., Fujita, N., Oomori, H., Noda, T., Haraguchi, T., Hiraoka, Y., et al. (2013) · Nature · doi:10.1038/nature11910 · Cited by 1,683
Rab Conversion as a Mechanism of Progression from Early to Late Endosomes
Rink, J. C., Ghigo, É., Kalaidzidis, Y. L., & Zerial, M. (2005) · Cell · doi:10.1016/j.cell.2005.06.043 · Cited by 1,680
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638
The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
Raiborg, C., & Stenmark, H. (2009) · Nature · doi:10.1038/nature07961 · Cited by 1,359
Self-citation
ERM proteins and merlin: integrators at the cell cortex
Bretscher, A., Edwards, K., & Fehon, R. G. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm882 · Cited by 1,306
EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
Simonsen, A., Lippe, R., Christoforidis, S., Gaullier, J.-M., Brech, A., Callaghan, J., Toh, B.-H., Murphy, C., Zerial, M., & Stenmark, H. (1998) · Nature · doi:10.1038/28879 · Cited by 1,133
Self-citation
Shaping cups into phagosomes and macropinosomes
Swanson, J. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2447 · Cited by 941
Essential Role of Phosphoinositide Metabolism in Synaptic Vesicle Recycling
Cremona, O., Paolo, G. D., Wenk, M. R., Lüthi, A., Kim, W. T., Takei, K., DANIELL, L. W., Nemoto, Y., Shears, S. B., Flavell, R. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)81649-9 · Cited by 836
The Beclin 1–VPS34 complex – at the crossroads of autophagy and beyond
Funderburk, S. F., Wang, Q. J., & Yue, Z. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.03.002 · Cited by 804
A Four-Step Cycle Driven by PI(4)P Hydrolysis Directs Sterol/PI(4)P Exchange by the ER-Golgi Tether OSBP
Mesmin, B., Bigay, J., von Filseck, J. M., Lacas‐Gervais, S., Drin, G., & Antonny, B. (2013) · Cell · doi:10.1016/j.cell.2013.09.056 · Cited by 798
Role of Substrates and Products of PI 3-kinase in Regulating Activation of Rac-Related Guanosine Triphosphatases by Vav
Han, J., Luby‐Phelps, K., Das, B., Shu, X., Xia, Y., Mosteller, R. D., Krishna, U. M., Falck, J. R., White, M. A., & Broek, D. (1998) · Science · doi:10.1126/science.279.5350.558 · Cited by 792
Dynamin-mediated Internalization of Caveolae
Henley, J. R., Krueger, E. W. A., Oswald, B. J., & McNiven, M. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.1.85 · Cited by 767
Parallels Between Cytokinesis and Retroviral Budding: A Role for the ESCRT Machinery
Carlton, J. G., & Martin-Serrano, J. (2007) · Science · doi:10.1126/science.1143422 · Cited by 764
Identification of the Switch in Early-to-Late Endosome Transition
Poteryaev, D., Datta, S., Ackema, K., Zerial, M., & Spang, A. (2010) · Cell · doi:10.1016/j.cell.2010.03.011 · Cited by 752
Dynamin at the Neck of Caveolae Mediates Their Budding to Form Transport Vesicles by GTP-driven Fission from the Plasma Membrane of Endothelium
Oh, P., McIntosh, D. P., & Schnitzer, J. E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.1.101 · Cited by 677
N‐WASP, a novel actin‐depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2‐dependent manner downstream of tyrosine kinases.
Miki, H., Miura, K., & Takenawa, T. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00917.x · Cited by 672
Simultaneous Binding of PtdIns(4,5)P 2 and Clathrin by AP180 in the Nucleation of Clathrin Lattices on Membranes
Ford, M. G. J., Pearse, B. M. F., Higgins, M. K., Vallis, Y., Owen, D. J., Gibson, A., Hopkins, C. R., Evans, P. R., & McMahon, H. T. (2001) · Science · doi:10.1126/science.291.5506.1051 · Cited by 659
Steering cell migration: lamellipodium dynamics and the regulation of directional persistence
Krause, M., & Gautreau, A. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3861 · Cited by 609
Ultrafast endocytosis at mouse hippocampal synapses
Watanabe, S., Rost, B. R., Camacho-Pérez, M., Davis, M. W., Söhl-Kielczynski, B., Rosenmund, C., & Jorgensen, E. M. (2013) · Nature · doi:10.1038/nature12809 · Cited by 607
Canonical and non-canonical autophagy: variations on a common theme of self-eating?
Codogno, P., Mehrpour, M., & Proikas‐Cezanne, T. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3249 · Cited by 563
Phosphatidylinositol-3-OH kinases are Rab5 effectors
Christoforidis, S., Miaczynska, M., Ashman, K., Wilm, M., Zhao, L., Yip, S.-C., Waterfield, M. D., Backer, J. M., & Zerial, M. (1999) · Nature Cell Biology · doi:10.1038/12075 · Cited by 559
Endophilin marks and controls a clathrin-independent endocytic pathway
Boucrot, E., Ferreira, A. P. A., Almeida-Souza, L., Debard, S., Vallis, Y., Howard, G., Bertot, L., Sauvonnet, N., & McMahon, H. T. (2015) · Nature · doi:10.1038/nature14067 · Cited by 542
Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis
Botelho, R. J., Teruel, M., Dierckman, R., Anderson, R., Wells, A., York, J. D., Meyer, T., & Grinstein, S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.7.1353 · Cited by 539
Osh Proteins Regulate Phosphoinositide Metabolism at ER-Plasma Membrane Contact Sites
Stefan, C. J., Manford, A. G., Baird, D., Yamada-Hanff, J., Mao, Y., & Emr, S. D. (2011) · Cell · doi:10.1016/j.cell.2010.12.034 · Cited by 499
Coordination of Rab8 and Rab11 in primary ciliogenesis
Knödler, A., Feng, S., Zhang, J., Zhang, X., Das, A. K., Peränen, J., & Guo, W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002401107 · Cited by 491
FCHo Proteins Are Nucleators of Clathrin-Mediated Endocytosis
Henne, W. M., Boucrot, E., Meinecke, M., Evergren, E., Vallis, Y., Mittal, R., & McMahon, H. T. (2010) · Science · doi:10.1126/science.1188462 · Cited by 483
Synaptic Vesicle Endocytosis Impaired by Disruption of Dynamin-SH3 Domain Interactions
Shupliakov, O., Löw, P., Grabs, D., Gad, H., Chen, H., David, C., Takei, K., Camilli, P. V. D., & Brodin, L. (1997) · Science · doi:10.1126/science.276.5310.259 · Cited by 481
P-Rex1, a PtdIns(3,4,5)P3- and Gβγ-Regulated Guanine-Nucleotide Exchange Factor for Rac
Welch, H. C. E., Coadwell, W. J., Ellson, C. D., Ferguson, G. J., Andrews, S., Erdjument‐Bromage, H., Tempst, P., Hawkins, P. T., & Stephens, L. (2002) · Cell · doi:10.1016/s0092-8674(02)00663-3 · Cited by 481
Role of the ENTH Domain in Phosphatidylinositol-4,5-Bisphosphate Binding and Endocytosis
Itoh, T., Koshiba, S., Kigawa, T., Kikuchi, A., Yokoyama, S., & Takenawa, T. (2001) · Science · doi:10.1126/science.291.5506.1047 · Cited by 469
Synaptic Vesicle Endocytosis
Saheki, Y., & De Camilli, P. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005645 · Cited by 457
Sorting Nexin-1 Mediates Tubular Endosome-to-TGN Transport through Coincidence Sensing of High- Curvature Membranes and 3-Phosphoinositides
Carlton, J., Bujny, M., Peter, B. J., Oorschot, V. M. J., Rutherford, A., Mellor, H., Klumperman, J., McMahon, H. T., & Cullen, P. J. (2004) · Current Biology · doi:10.1016/j.cub.2004.09.077 · Cited by 441
Repeated ER–endosome contacts promote endosome translocation and neurite outgrowth
Raiborg, C., Wenzel, E. M., Pedersen, N. M., Olsvik, H. L., Schink, K. O., Schultz, S. W., Vietri, M., Nisi, V., Bucci, C., Brech, A., et al. (2015) · Nature · doi:10.1038/nature14359 · Cited by 436
Self-citation
Spatiotemporal control of endocytosis by phosphatidylinositol-3,4-bisphosphate
Posor, Y., Eichhorn‐Grünig, M., Puchkov, D., Schöneberg, J., Ullrich, A., Lampe, A., Müller, R., Zarbakhsh, S., Gulluni, F., Hirsch, E., et al. (2013) · Nature · doi:10.1038/nature12360 · Cited by 414
An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway
Shin, H., Hayashi, M., Christoforidis, S., Lacas‐Gervais, S., Hoepfner, S., Wenk, M. R., Modregger, J., Uttenweiler‐Joseph, S., Wilm, M. S., Nystuen, A., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505128 · Cited by 409
Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers
de Saint-Jean, M., Delfosse, V., Douguet, D., Chicanne, G., Payrastre, B., Bourguet, W., Antonny, B., & Drin, G. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201104062 · Cited by 404
Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate
von Filseck, J. M., Čopič, A., Delfosse, V., Vanni, S., Jackson, C. L., Bourguet, W., & Drin, G. (2015) · Science · doi:10.1126/science.aab1346 · Cited by 388
Cholesterol transport through lysosome-peroxisome membrane contacts.
Chu, B.-B., Liao, Y.-C., Qi, W., Xie, C., Du, X., Wang, J., Yang, H., Miao, H.-H., Li, B.-L., & Song, B.-L. (2015) · Cell · doi:10.1016/j.cell.2015.02.019 · Cited by 377
Exo70 interacts with phospholipids and mediates the targeting of the exocyst to the plasma membrane
He, B., Xi, F., Zhang, X., Zhang, J., & Guo, W. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601834 · Cited by 337
A Phosphoinositide Switch Controls the Maturation and Signaling Properties of APPL Endosomes
Zoncu, R., Perera, R. M., Balkin, D. M., Pirruccello, M., Toomre, D. K., & Camilli, P. V. D. (2009) · Cell · doi:10.1016/j.cell.2009.01.032 · Cited by 336
ESCRTs and Fab1 Regulate Distinct Steps of Autophagy
Rusten, T. E., Vaccari, T., Lindmo, K., Rodahl, L. M., Nezis, I. P., Sem-Jacobsen, C., Wendler, F., Vincent, J., Brech, A., Bilder, D. H., et al. (2007) · Current Biology · doi:10.1016/j.cub.2007.09.032 · Cited by 332
Self-citation
Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae
Suzuki, K., Akioka, M., Kondo‐Kakuta, C., Yamamoto, H., & Ohsumi, Y. (2013) · Journal of Cell Science · doi:10.1242/jcs.122960 · Cited by 330
Modulation of Receptor Recycling and Degradation by the Endosomal Kinesin KIF16B
Hoepfner, S., Severin, F. F., Cabezas, A., Habermann, B. H., Runge, A., Gillooly, D. J., Stenmark, H., & Zerial, M. (2005) · Cell · doi:10.1016/j.cell.2005.02.017 · Cited by 327
Self-citation
A TRP Channel in the Lysosome Regulates Large Particle Phagocytosis via Focal Exocytosis
Samie, M., Wang, X., Zhang, X., Goschka, A., Li, X., Cheng, X., Gregg, E., Azar, M., Yue, Z., Garrity, A. G., et al. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.08.003 · Cited by 324
Sec2p Mediates Nucleotide Exchange on Sec4p and Is Involved in Polarized Delivery of Post-Golgi Vesicles
Walch-Solimena, C., Collins, R., & Novick, P. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.7.1495 · Cited by 321
FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes
Raiborg, C., Bremnes, B., Mehlum, A., Gillooly, D. J., D’Arrigo, A., Stang, E., & Stenmark, H. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.12.2255 · Cited by 319
Self-citation
Phosphoinositides regulate ion channels
Hille, B., Dickson, E. J., Kruse, M., Vivas, O., & Suh, B.-C. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.09.010 · Cited by 312
Dynamin: functional design of a membrane fission catalyst.
Schmid, S., & Frolov, V. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104016 · Cited by 292
Dynamin 2 Is Required for Phagocytosis in Macrophages
Gold, E. S., Underhill, D. M., Morrissette, N. S., Guo, J., McNiven, M. A., & Aderem, A. A. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.12.1849 · Cited by 286
Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: Structures, functions and roles in disease
Teasdale, R. D., & Collins, B. M. (2012) · Biochemical Journal · doi:10.1042/bj20111226 · Cited by 281
Restricted Accumulation of Phosphatidylinositol 3-Kinase Products in a Plasmalemmal Subdomain during Fcγ Receptor-Mediated Phagocytosis
Marshall, J. G., Booth, J. W., Stambolic, V., Mak, T. W., Balla, T., Schreiber, A. D., Meyer, T., & Grinstein, S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.7.1369 · Cited by 281
Phosphoinositide 3-kinase activates Rac by entering in a complex with Eps8, Abi1, and Sos-1
Innocenti, M., Frittoli, E., Ponzanelli, I., Falck, J. R., Brachmann, S. M., Fiore, P. P. D., & Scita, G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200206079 · Cited by 267
Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
Zhang, X., Orlando, K., He, B., Xi, F., Zhang, J., Zajac, A. L., & Guo, W. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200704128 · Cited by 266
Polyphosphoinositide binding domains: Key to inositol lipid biology
Hammond, G. R. V., & Balla, T. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2015.02.013 · Cited by 258
PI(5)P Regulates Autophagosome Biogenesis
Vicinanza, M., Korolchuk, V. I., Ashkenazi, A., Puri, C., Menzies, F. M., Clarke, J. H., & Rubinsztein, D. C. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.007 · Cited by 256
The GTPase-Activating Protein GRAF1 Regulates the CLIC/GEEC Endocytic Pathway
Lundmark, R., Doherty, G. J., Howes, M. T., Cortese, K., Vallis, Y., Parton, R. G., & McMahon, H. T. (2008) · Current Biology · doi:10.1016/j.cub.2008.10.044 · Cited by 253
Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
Stroupe, C., Collins, K. M., Fratti, R. A., & Wickner, W. T. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601051 · Cited by 244
ESCRT-I Core and ESCRT-II GLUE Domain Structures Reveal Role for GLUE in Linking to ESCRT-I and Membranes
Teo, H., Gill, D. J., Sun, J., Perisic, O., Veprintsev, D. B., Vallis, Y., Emr, S. D., & Williams, R. L. (2006) · Cell · doi:10.1016/j.cell.2006.01.047 · Cited by 242
PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody
Sagona, A. P., Nezis, I. P., Pedersen, N. M., Liestøl, K., Poulton, J., Rusten, T. E., Skotheim, R. I., Raiborg, C., & Stenmark, H. (2010) · Nature Cell Biology · doi:10.1038/ncb2036 · Cited by 239
Self-citation
In vivo, Pikfyve generates PI(3,5)P 2 , which serves as both a signaling lipid and the major precursor for PI5P
Zolov, S. N., Bridges, D., Zhang, Y., Lee, W.-W., Riehle, E., Verma, R., Lenk, G. M., Converso-Baran, K., Weide, T., Albin, R. L., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203106109 · Cited by 236
A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signalling
Côté, J., Motoyama, A. B., Bush, J., & Vuori, K. (2005) · Nature Cell Biology · doi:10.1038/ncb1280 · Cited by 231
Phosphatidylinositol 4,5-Bisphosphate Mediates the Targeting of the Exocyst to the Plasma Membrane for Exocytosis in Mammalian Cells
Liu, J., Zuo, X., Yue, P., & Guo, W. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-05-0461 · Cited by 227
The Rab5 Effector Rabankyrin-5 Regulates and Coordinates Different Endocytic Mechanisms
Schnatwinkel, C., Christoforidis, S., Lindsay, M. R., Uttenweiler‐Joseph, S., Wilm, M. S., Parton, R. G., & Zerial, M. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020261 · Cited by 225
Phosphoinositide 3-kinase enables phagocytosis of large particles by terminating actin assembly through Rac/Cdc42 GTPase-activating proteins
Schlam, D., Bagshaw, R. D., Freeman, S. A., Collins, R. F., Pawson, T. J., Fairn, G. D., & Grinstein, S. (2015) · Nature Communications · doi:10.1038/ncomms9623 · Cited by 222
Multivesicular body morphogenesis requires phosphatidyl-inositol 3-kinase activity
Fernandez‐Borja, M., Wubbolts, R., Calafat, J., Janssen, H., Divecha, N., Dusseljee, S., & Neefjes, J. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80048-7 · Cited by 214
Direct association of Bazooka/PAR-3 with the lipid phosphatase PTEN reveals a link between the PAR/aPKC complex and phosphoinositide signaling
von Stein, W., Ramrath, A., Grimm, A., Müller-Borg, M., & Wodarz, A. (2005) · Development · doi:10.1242/dev.01720 · Cited by 213
PI3K Class II α Controls Spatially Restricted Endosomal PtdIns3P and Rab11 Activation to Promote Primary Cilium Function
Franco, I., Gulluni, F., Campa, C. C., Costa, C., Margaria, J. P., Ciraolo, E., Martini, M., Monteyne, D., Luca, E. D., Germena, G., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.01.022 · Cited by 209
Requirements for Vav guanine nucleotide exchange factors and Rho GTPases in FcgammaR- and complement-mediated phagocytosis.
Hall, A. B., Gakidis, M. A. M., Glogauer, M., Wilsbacher, J., Gao, S., Swat, W., & Brugge, J. (2006) · Immunity · doi:10.1016/j.immuni.2006.02.005 · Cited by 207
A Rab8-specific GDP/GTP Exchange Factor Is Involved in Actin Remodeling and Polarized Membrane Transport
Hattula, K., Furuhjelm, J., Arffman, A., & Peränen, J. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-03-0143 · Cited by 205
A Polybasic Motif Allows N-WASP to Act as a Sensor of PIP2 Density
Papayannopoulos, V., Co, C., Prehoda, K. E., Snapper, S. B., Taunton, J., & Lim, W. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.11.054 · Cited by 205
Eap45 in Mammalian ESCRT-II Binds Ubiquitin via a Phosphoinositide-interacting GLUE Domain
Slagsvold, T., Aasland, R., Hirano, S., Bache, K. G., Raiborg, C., Trambaiolo, D. M., Wakatsuki, S., & Stenmark, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501510200 · Cited by 199
Self-citation
Phosphoinositides in Cell ArchitecturePreprint
Shewan, A. M., Eastburn, D. J., & Mostov, K. E. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004796 · Cited by 194
Wiskott-Aldrich syndrome protein is necessary for efficient IgG-mediated phagocytosis
Lorenzi, R., Brickell, P. M., Katz, D. R., Kinnon, C., & Thrasher, A. J. (2000) · Blood · doi:10.1182/blood.v95.9.2943.009k17_2943_2946 · Cited by 192
A phosphoinositide conversion mechanism for exit from endosomes
Ketel, K., Krauss, M., Nicot, A.-S., Puchkov, D., Wieffer, M., Müller, R., Subramanian, D., Schultz, C., Laporte, J., & Haucke, V. (2016) · Nature · doi:10.1038/nature16516 · Cited by 189
PDZ Domains of Par-3 as Potential Phosphoinositide Signaling Integrators
Wu, H., Feng, W., Chen, J., Chan, L.-N., Huang, S., & Zhang, M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.10.028 · Cited by 183
SNX–BAR proteins in phosphoinositide-mediated, tubular-based endosomal sorting
van Weering, J. R. T., Verkade, P., & Cullen, P. J. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2009.11.009 · Cited by 175
SNX–BAR‐Mediated Endosome Tubulation is Co‐ordinated with Endosome Maturation
van Weering, J. R. T., Verkade, P., & Cullen, P. J. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01297.x · Cited by 172
A phosphatidylinositol (4,5)-bisphosphate binding site within μ2-adaptin regulates clathrin-mediated endocytosis
Rohde, G., Wenzel, D., & Haucke, V. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200203103 · Cited by 171
Myosin V Transports Secretory Vesicles via a Rab GTPase Cascade and Interaction with the Exocyst Complex
Jin, Y., Sultana, A., Gandhi, P., Franklin, E., Hamamoto, S., Khan, A. R., Munson, M., Schekman, R. W., & Weisman, L. S. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.10.009 · Cited by 163
Triggered Ca2+ influx is required for extended synaptotagmin 1‐induced ER‐plasma membrane tethering
Idevall-Hagren, O., Lu, A., Xie, B.-C., & Camilli, P. D. (2015) · EMBO Journal · doi:10.15252/embj.201591565 · Cited by 160
Regulation of nutrient-sensitive autophagy by uncoordinated 51-like kinases 1 and 2
McAlpine, F. E., Williamson, L. E., Tooze, S. A., & Chan, E. Y. W. (2013) · Autophagy · doi:10.4161/auto.23066 · Cited by 158
Insulin induces phosphatidylinositol‐3‐phosphate formation through TC10 activation
Maffucci, T., Brancaccio, A., Piccolo, E., Stein, R. C., & Falasca, M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg402 · Cited by 157
Transport of phosphatidylinositol 3‐phosphate into the vacuole via autophagic membranes in Saccharomyces cerevisiae
Obara, K., Noda, T., Niimi, K., & Ohsumi, Y. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01188.x · Cited by 150
Phosphoinositides in phagocytosis and macropinocytosis
Levin‐Konigsberg, R., Grinstein, S., & Schlam, D. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.09.005 · Cited by 150
Membrane Targeting of Bazooka/PAR-3 Is Mediated by Direct Binding to Phosphoinositide Lipids
Krahn, M. P., Klopfenstein, D. R., Fischer, N., & Wodarz, A. (2010) · Current Biology · doi:10.1016/j.cub.2010.01.065 · Cited by 148
Phosphatidylinositol 4-Phosphate Controls Both Membrane Recruitment and a Regulatory Switch of the Rab GEF Sec2p
Mizuno-Yamasaki, E., Medkova, M., Coleman, J., & Novick, P. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.03.016 · Cited by 148
Molecular basis for coupling the plasma membrane to the actin cytoskeleton during clathrin-mediated endocytosis
Skružný, M., Brach, T., Ciuffa, R., Rybina, S., Wachsmuth, M., & Kaksonen, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207011109 · Cited by 148
Recruitment of OCRL and Inpp5B to phagosomes by Rab5 and APPL1 depletes phosphoinositides and attenuates Akt signaling
Bohdanowicz, M., Balkin, D. M., Camilli, P. V. D., & Grinstein, S. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-06-0489 · Cited by 146
Lipid Products of Phosphoinositide 3-Kinase Bind Human Profilin with High Affinity
Lu, P., Shieh, W.-R., Rhee, S. G., Yin, H. L., & Chen, C. (1996) · Biochemistry · doi:10.1021/bi961878z · Cited by 143
Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15
Hirst, J., Borner, G. H. H., Edgar, J. R., Hein, M. Y., Mann, M., Buchholz, F., Antrobus, R., & Robinson, M. S. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-03-0170 · Cited by 129
PI(4,5)P2-binding effector proteins for vesicle exocytosis
Martin, T. F. J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.09.017 · Cited by 124
A role of OCRL in clathrin-coated pit dynamics and uncoating revealed by studies of Lowe syndrome cells
Nández, R., Balkin, D. M., Messa, M., Liang, L., Paradise, S., Czapla, H., Hein, M. Y., Duncan, J. S., Mann, M., & Camilli, P. V. D. (2014) · eLife · doi:10.7554/elife.02975 · Cited by 122
The HOPS Proteins hVps41 and hVps39 Are Required for Homotypic and Heterotypic Late Endosome Fusion
Pols, M. S., ten Brink, C., Gosavi, P., Oorschot, V. M. J., & Klumperman, J. (2012) · Traffic · doi:10.1111/tra.12027 · Cited by 117
Sequential breakdown of 3-phosphorylated phosphoinositides is essential for the completion of macropinocytosis
Maekawa, M., Shimpei, T., Mochizuki, Y., Kawai, K., Ikeda, Y., Araki, N., Skolnik, E. Y., Taguchi, T., & Arai, H. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311029111 · Cited by 110
Phosphatidylinositol 4-Phosphate Formation at ER Exit Sites Regulates ER Export
Blumental‐Perry, A., Haney, C. J., Weixel, K. M., Watkins, S. C., Weisz, O. A., & Aridor, M. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.09.001 · Cited by 110
Class III phosphatidylinositol 3–kinase and its catalytic product P tdIns3 P in regulation of endocytic membrane traffic
Raiborg, C., Schink, K. O., & Stenmark, H. (2013) · FEBS Journal · doi:10.1111/febs.12116 · Cited by 107
Self-citation
PIKfyve Inhibition Interferes with Phagosome and Endosome Maturation in Macrophages
Kim, G. H. E., Dayam, R. M., Prashar, A., Terebiznik, M. R., & Botelho, R. J. (2014) · Traffic · doi:10.1111/tra.12199 · Cited by 105
On the move: organelle dynamics during mitosis
Jongsma, M. L. M., Berlin, I., & Neefjes, J. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.10.005 · Cited by 103
Structural basis for the Rho- and phosphoinositide-dependent localization of the exocyst subunit Sec3
Yamashita, M., Kurokawa, K., Sato, Y., Yamagata, A., Mimura, H., Yoshikawa, A., Sato, K., Nakano, A., & Fukai, S. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1722 · Cited by 103
A Hereditary Spastic Paraplegia Mouse Model Supports a Role of ZFYVE26/SPASTIZIN for the Endolysosomal System
Khundadze, M., Kollmann, K., Koch, N., Biskup, C. U., Nietzsche, S., Zimmer‐Bensch, G., Hennings, J. C., Huebner, A. K., Symmank, J., Jahić, A., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003988 · Cited by 100
Tubular endocytosis drives remodelling of the apical surface during epithelial morphogenesis in Drosophila
Fabrowski, P., Necakov, A., Mumbauer, S., Loeser, E., Reversi, A., Streichan, S. J., Briggs, J., & de Renzis, S. (2013) · Nature Communications · doi:10.1038/ncomms3244 · Cited by 98
Omegasomes: PI3P platforms that manufacture autophagosomes
Roberts, R. L., & Ktistakis, N. T. (2013) · Essays in Biochemistry · doi:10.1042/bse0550017 · Cited by 98
Compartmental signal modulation: Endosomal phosphatidylinositol 3-phosphate controls endosome morphology and selective cargo sorting
Fili, N., Calleja, V., Woscholski, R., Parker, P. J., & Larijani, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607040103 · Cited by 96
Rho GTPases, phosphoinositides, and actin
Croisé, P., Estay-Ahumada, C. E., Gasman, S., & Ory, S. (2014) · Small GTPases · doi:10.4161/sgtp.29469 · Cited by 95
Phosphoinositides: Lipids with informative heads and mastermind functions in cell division
Cauvin, C., & Échard, A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.10.013 · Cited by 90
PIP3-dependent macropinocytosis is incompatible with chemotaxis
Veltman, D. M., Lemieux, M. G., Knecht, D. A., & Insall, R. H. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201309081 · Cited by 89
The membrane-associated proteins FCHo and SGIP are allosteric activators of the AP2 clathrin adaptor complex
Hollopeter, G., Lange, J. J., Zhang, Y., Vu, T. N., Gu, M., Ailion, M., Lambie, E. J., Slaughter, B. D., Unruh, J. R., Florens, L. A., et al. (2014) · eLife · doi:10.7554/elife.03648 · Cited by 88
Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2
Pechstein, A., Bacetic, J., Vahedi‐Faridi, A., Gromova, K. V., Sundborger, A., Tomlin, N., Krainer, G., Vorontsova, O. V., Schäfer, J. G., Owe, S. G., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911073107 · Cited by 85
PtdIns(3,4,5)P 3 is a regulator of myosin-X localization and filopodia formation
Plantard, L., Arjonen, A., Lock, J. G., Nurani, G., Ivaska, J., & Strömblad, S. (2010) · Journal of Cell Science · doi:10.1242/jcs.069609 · Cited by 84
Phosphatidylinositol 5-phosphate regulates invasion through binding and activation of Tiam1
Viaud, J., Lagarrigue, F., Ramel, D., Allart, S., Chicanne, G., Ceccato, L., Courilleau, D., Xuereb, J.-M., Pertz, O. C., Payrastre, B., et al. (2014) · Nature Communications · doi:10.1038/ncomms5080 · Cited by 81
Nuclear phosphoinositides and their impact on nuclear functions
Shah, Z. H., Jones, D. R., Sommer, L., Foulger, R., Bultsma, Y., D’Santos, C. S., & Divecha, N. (2013) · FEBS Journal · doi:10.1111/febs.12543 · Cited by 81
Production of phosphatidylinositol 5‐phosphate via PIKfyve and MTMR3 regulates cell migration
Oppelt, A., Lobert, V. H., Haglund, K., Mackey, A. M., Rameh, L. E., Liestøl, K., Schink, K. O., Pedersen, N. M., Wenzel, E. M., Haugsten, E. M., et al. (2012) · EMBO Reports · doi:10.1038/embor.2012.183 · Cited by 81
Self-citation
Differential Association of Phosphatidylinositol 3-Kinase, SHIP-1, and PTEN with Forming Phagosomes
Kamen, L. A., Levinsohn, J. L., & Swanson, J. A. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0061 · Cited by 79
Inactivation of the Class II PI3K-C2β Potentiates Insulin Signaling and Sensitivity
Alliouachene, S., Bilanges, B., Chicanne, G., Anderson, K. E., Pearce, W., Ali, K., Valet, C., Posor, Y., Low, P. C., Chaussade, C., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.052 · Cited by 75
Phosphatidylinositol 4-phosphate and phosphatidylinositol 3-phosphate regulate phagolysosome biogenesis
Jeschke, A., Zehethofer, N., Lindner, B., Krupp, J., Schwudke, D., Haneburger, I., Jović, M., Backer, J., Balla, T., Hilbi, H., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1423456112 · Cited by 73
Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1
Srivastava, S., Choudhury, P., Li, Z., Liu, G., Nadkarni, V., Ko, K. A., Coetzee, W. A., & Skolnik, E. Y. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-08-0763 · Cited by 73
Genetic Analysis of the Myotubularin Family of Phosphatases in Caenorhabditis elegans
Xue, Y., Fares, H., Grant, B. D., Li, Z., Rose, A. M., Clark, S. G., & Skolnik, E. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303259200 · Cited by 73
TOM1 is a PI5P effector involved in the regulation of endosomal maturation
Boal, F., Mansour, R., Gayral, M., Saland, E., Chicanne, G., Xuereb, J.-M., Marcellin, M., Burlet‐Schiltz, O., Sansonetti, P. J., Payrastre, B., et al. (2015) · Journal of Cell Science · doi:10.1242/jcs.166314 · Cited by 72
The epsin protein family: coordinators of endocytosis and signaling
Sen, A., Madhivanan, K., Mukherjee, D., & Aguilar, R. C. (2012) · BioMolecular Concepts · doi:10.1515/bmc-2011-0060 · Cited by 69
Molecular Mechanism of Cholesterol- and Polyphosphoinositide-Mediated Syntaxin Clustering
Murray, D. H., & Tamm, L. K. (2011) · Biochemistry · doi:10.1021/bi201307u · Cited by 67
Atg24-assisted mitophagy in the foot cells is necessary for proper asexual differentiation inMagnaporthe oryzae
He, Y., Deng, Y., & Naqvi, N. I. (2013) · Autophagy · doi:10.4161/auto.26057 · Cited by 66
Phosphoinositides in the regulation of actin cortex and cell migration
Tsujita, K., & Itoh, T. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.10.011 · Cited by 66
Triggering Actin Comets Versus Membrane Ruffles: Distinctive Effects of Phosphoinositides on Actin Reorganization
Ueno, T., Falkenburger, B. H., Pohlmeyer, C. W., & Inoue, T. (2011) · Science Signaling · doi:10.1126/scisignal.2002033 · Cited by 64
Membrane recruitment of DOCK180 by binding to PtdIns(3,4,5)P3
KOBAYASHI, S., Shirai, T., Kiyokawa, E., Mochizuki, N., Matsuda, M., & Fukui, Y. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3540073 · Cited by 64
The kinesin KIF16B mediates apical transcytosis of transferrin receptor in AP-1B-deficient epithelia
Perez Bay, A. E., Schreiner, R., Mazzoni, F., Carvajal‐Gonzalez, J. M., Gravotta, D., Perret, E., Lehmann Mantaras, G., Zhu, Y., & Rodriguez‐Boulan, E. J. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.130 · Cited by 63
A role for SNX5 in the regulation of macropinocytosis
Lim, J. P., Wang, J. T. H., Kerr, M. C., Teasdale, R. D., & Gleeson, P. A. (2008) · BMC Cell Biology · doi:10.1186/1471-2121-9-58 · Cited by 63
Pairing phosphoinositides with calcium ions in endolysosomal dynamics
Shen, D., Wang, X., & Xu, H. (2011) · BioEssays · doi:10.1002/bies.201000152 · Cited by 62
PI3P phosphatase activity is required for autophagosome maturation and autolysosome formation
Wu, Y., Cheng, S., Zhao, H., Zou, W., Yoshina, S., Mitani, S., Zhang, H., & Wang, X. (2014) · EMBO Reports · doi:10.15252/embr.201438618 · Cited by 61
Microtubule motors mediate endosomal sorting by maintaining functional domain organization.
Hunt, S. D., Townley, A. K., Danson, C. M., Cullen, P. J., & Stephens, D. J. (2013) · Journal of Cell Science · doi:10.1242/jcs.122317 · Cited by 57
WIPI-Mediated Autophagy and Longevity
Grimmel, M., Backhaus, C., & Proikas‐Cezanne, T. (2015) · Cells · doi:10.3390/cells4020202 · Cited by 56
The Fab1/PIKfyve Phosphoinositide Phosphate Kinase Is Not Necessary to Maintain the pH of Lysosomes and of the Yeast Vacuole
Ho, C. Y., Choy, C. H., Wattson, C. A., Johnson, D., & Botelho, R. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.613984 · Cited by 56
Phosphatidylinositol 3,4,5-trisphosphate Localization in Recycling Endosomes Is Necessary for AP-1B–dependent Sorting in Polarized Epithelial Cells
Fields, I. C., King, S. M., Shteyn, E., Kang, R. S., & Fölsch, H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-01-0036 · Cited by 56
Osh4p is needed to reduce the level of phosphatidylinositol-4-phosphate on secretory vesicles as they mature
Ling, Y., Hayano, S., & Novick, P. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-06-1087 · Cited by 55
Phosphoinositides differentially regulate alpha-actinin flexibility and function
Corgan, A. M., Singleton, C., SANTOSO, C. B., & Greenwood, J. A. (2004) · Biochemical Journal · doi:10.1042/bj20031124 · Cited by 55
Removal or masking of phosphatidylinositol(4,5)bisphosphate from the outer mitochondrial membrane causes mitochondrial fragmentation
Rosivatz, E., & Woscholski, R. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.10.025 · Cited by 54
PIKfyve, MTMR3 and their product PtdIns5P regulate cancer cell migration and invasion through activation of Rac1
Oppelt, A., Haugsten, E. M., Zech, T., Danielsen, H. E., Sveen, A., Lobert, V. H., Skotheim, R. I., & Wesche, J. (2014) · Biochemical Journal · doi:10.1042/bj20140132 · Cited by 51
CRISPR‐Cas9: how research on a bacterial RNA‐guided mechanism opened new perspectives in biotechnology and biomedicine
Charpentier, E. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201504847 · Cited by 48
Phosphoinositide Function in Cytokinesis
Brill, J. A., Wong, R., & Wilde, A. (2011) · Current Biology · doi:10.1016/j.cub.2011.10.001 · Cited by 48
The Chemical Biology of Phosphoinositide 3‐Kinases
Wymann, M. P., & Schultz, C. (2012) · ChemBioChem · doi:10.1002/cbic.201200089 · Cited by 43
Endocytic membrane turnover at the leading edge is driven by a transient interaction between Cdc42 and GRAF1
Francis, M. K., Holst, M. R., Vidal‐Quadras, M., Henriksson, S., Santarella‐Mellwig, R., Sandblad, L., & Lundmark, R. (2015) · Journal of Cell Science · doi:10.1242/jcs.174417 · Cited by 40
Nuclear Envelope Formation: Mind the Gaps
Larijani, B., & Poccia, D. (2009) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133625 · Cited by 34
Phosphorylation of the Rab exchange factor Sec2p directs a switch in regulatory binding partners
Stalder, D., Mizuno-Yamasaki, E., Ghassemian, M., & Novick, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320029110 · Cited by 32
Requirement for Golgi-localized PI(4)P in fusion of COPII vesicles with Golgi compartments
Lorente-Rodríguez, A., & Barlowe, C. K. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-04-0317 · Cited by 31
Phosphoinositides in membrane contact sites
Raiborg, C., Wenzel, E. M., Pedersen, N. M., & Stenmark, H. (2016) · Biochemical Society Transactions · doi:10.1042/bst20150190 · Cited by 29
Self-citation
ESCRT-0 marks an APPL1-independent transit route for EGFR between the cell surface and the EEA1-positive early endosome
Rodriguez, N. F., Kenwright, D. A., Chung, P., Harrison, A. W., Stefani, F., Waigh, T. A., Allan, V., & Woodman, P. G. (2015) · Journal of Cell Science · doi:10.1242/jcs.161786 · Cited by 28
SNAREs, HOPS, and regulatory lipids control the dynamics of vacuolar actin during homotypic fusion
Karunakaran, S., Sasser, T., Rajalekshmi, S., & Fratti, R. A. (2012) · Journal of Cell Science · doi:10.1242/jcs.091900 · Cited by 25
Phosphoinositides in Chemotaxis
Weiger, M. C., & Parent, C. A. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-3015-1_7 · Cited by 23
Phosphoinositides Function Asymmetrically for Membrane Fusion, Promoting Tethering and 3Q-SNARE Subcomplex Assembly
Xu, H., & Wickner, W. T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.183111 · Cited by 20
A Stretch of Polybasic Residues Mediates Cdc42 GTPase-activating Protein (CdGAP) Binding to Phosphatidylinositol 3,4,5-Trisphosphate and Regulates Its GAP Activity
Karimzadeh, F., Primeau, M., Mountassif, D., Rouiller, I., & Lamarche‐Vane, N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.344606 · Cited by 17
Chemical intervention tools to probe phosphoinositide-dependent signalling
Woscholski, R. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140186 · Cited by 2

Flagged first, then by citations

1 of the 158 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

10.1042/bj3540073 · DOI

Sorted by citations

Exosomal lipid composition and the role of ether lipids and phosphoinositides in exosome biology
Skotland, T., Hessvik, N. P., Sandvig, K., & Llorente, A. (2019) · Journal of Lipid Research · doi:10.1194/jlr.r084343 · Cited by 730
An emerging focus on lipids in extracellular vesicles
Skotland, T., Sagini, K., Sandvig, K., & Llorente, A. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.03.002 · Cited by 578
PI3K isoforms in cell signalling and vesicle trafficking
Bilanges, B., Posor, Y., & Vanhaesebroeck, B. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0129-z · Cited by 535
Lysosome biogenesis: Regulation and functions
Yang, C., & Wang, X. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202102001 · Cited by 491
Early innate immune responses to bacterial LPS
Rosadini, C. V., & Kagan, J. C. (2016) · Current Opinion in Immunology · doi:10.1016/j.coi.2016.10.005 · Cited by 327
Mesenchymal–epithelial transition in development and reprogramming
Pei, D., Shu, X., Gassama‐Diagne, A., & Thiery, J. P. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0195-z · Cited by 306
Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance
Enkavi, G., Javanainen, M., Kulig, W., Róg, T., & Vattulainen, I. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00538 · Cited by 293
Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation
Muller, M. P., Jiang, T., Sun, C., Lihan, M., Pant, S., Mahinthichaichan, P., Trifan, A., & Tajkhorshid, E. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00608 · Cited by 282
Legionella and Coxiella effectors: strength in diversity and activity
Qiu, J., & Luo, Z. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.67 · Cited by 266
Phosphatidylinositol‐3‐phosphate in the regulation of autophagy membrane dynamics
Nascimbeni, A. C., Codogno, P., & Morel, É. (2016) · FEBS Journal · doi:10.1111/febs.13987 · Cited by 254
Neuronal lysosomal dysfunction releases exosomes harboring APP C-terminal fragments and unique lipid signatures
Miranda, A. M., Lasiecka, Z. M., Xu, Y., Neufeld, J., Shahriar, S., Simoes, S., Chan, R. B., Oliveira, T. G., Small, S. A., & Di Paolo, G. (2018) · Nature Communications · doi:10.1038/s41467-017-02533-w · Cited by 226
Life in the lumen: The multivesicular endosome
Grüenberg, J. (2019) · Traffic · doi:10.1111/tra.12715 · Cited by 223
Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane
Katan, M., & Cockcroft, S. (2020) · Essays in Biochemistry · doi:10.1042/ebc20200041 · Cited by 176
PI5P and PI(3,5)P2: Minor, but Essential Phosphoinositides
Hasegawa, J., Strunk, B. S., & Weisman, L. S. (2017) · Cell Structure and Function · doi:10.1247/csf.17003 · Cited by 165
TRPML1: The Ca(2+)retaker of the lysosome
Paola, S. D., Rosato, A. S., & Medina, D. L. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.06.006 · Cited by 162
The EGFR odyssey – from activation to destruction in space and time
Bakker, J., Spits, M., Neefjes, J., & Berlin, I. (2017) · Journal of Cell Science · doi:10.1242/jcs.209197 · Cited by 160
Beyond PI3Ks: targeting phosphoinositide kinases in disease
Burke, J. E., Triscott, J., Emerling, B. M., & Hammond, G. R. V. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00582-5 · Cited by 156
Phosphatidylinositol synthesis at the endoplasmic reticulum
Blunsom, N. J., & Cockcroft, S. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.05.015 · Cited by 116
ER as master regulator of membrane trafficking and organelle function
Wenzel, E. M., Elfmark, L. A., Stenmark, H., & Raiborg, C. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202205135 · Cited by 120
Self-citation
SKIP‐HOPS recruits TBC1D15 for a Rab7‐to‐Arl8b identity switch to control late endosome transport
Jongsma, M. L. M., Bakker, J., Cabukusta, B., Liv, N., van Elsland, D. M., Fermie, J., Akkermans, J. J. L. L., Kuijl, C. P., van der Zanden, S. Y., Janssen, L., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019102301 · Cited by 116
Regulation of actin dynamics by PI(4,5)P2 in cell migration and endocytosis
Senju, Y., & Lappalainen, P. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.08.003 · Cited by 101
Targeting PI3K family with small-molecule inhibitors in cancer therapy: current clinical status and future directions
Li, H., Wen, X., Ren, Y., Fan, Z., Zhang, J., He, G., & Fu, L. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02072-1 · Cited by 113
Membrane Traffic in the Late Steps of Cytokinesis
Frémont, S., & Échard, A. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.019 · Cited by 103
The role of PS 18:0/18:1 in membrane function
Skotland, T., & Sandvig, K. (2019) · Nature Communications · doi:10.1038/s41467-019-10711-1 · Cited by 99
Defining the subcellular distribution and metabolic channeling of phosphatidylinositol
Pemberton, J. G., Kim, Y. J., Humpolíčková, J., Eisenreichová, A., Sengupta, N., Tóth, D. J., Bouřa, E., & Balla, T. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201906130 · Cited by 97
Regulation of Autophagy Enzymes by Nutrient Signaling
King, K. E., Losier, T. T., & Russell, R. C. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.01.006 · Cited by 92
Robust and automated detection of subcellular morphological motifs in 3D microscopy images
Driscoll, M., Welf, E. S., Jamieson, A. R., Dean, K. M., Isogai, T., Fiolka, R. P., & Danuser, G. M. (2019) · Nature Methods · doi:10.1038/s41592-019-0539-z · Cited by 89
Phospholipase C families: Common themes and versatility in physiology and pathology
Katan, M., & Cockcroft, S. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101065 · Cited by 89
Neuronal endolysosomal transport and lysosomal functionality in maintaining axonostasis
Roney, J. C., Cheng, X., & Sheng, Z. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202111077 · Cited by 91
PI(4,5)P2: signaling the plasma membrane
Wills, R. C., & Hammond, G. R. V. (2022) · Biochemical Journal · doi:10.1042/bcj20220445 · Cited by 85
Identity and functions of inorganic and inositol polyphosphates in plants
Lorenzo‐Orts, L., Couto, D., & Hothorn, M. (2019) · New Phytologist · doi:10.1111/nph.16129 · Cited by 79
PI3KC2α-dependent and VPS34-independent generation of PI3P controls primary cilium-mediated autophagy in response to shear stress
Boukhalfa, A., Nascimbeni, A. C., Ramel, D., Dupont, N., Hirsch, E., Gayral, S., Laffargue, M., Codogno, P., & Morel, É. (2020) · Nature Communications · doi:10.1038/s41467-019-14086-1 · Cited by 83
Bioactive Lipids and Their Derivatives in Biomedical Applications
Park, J.-W., Choi, J., Kim, D., Lee, S., Lee, B., Lee, Y., Kim, S., Kwon, S., Noh, M., Lee, M., et al. (2021) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2021.107 · Cited by 86
Extracellular vesicle budding is inhibited by redundant regulators of TAT-5 flippase localization and phospholipid asymmetry
Beer, K. B., Rivas-Castillo, J., Kuhn, K. D., Fazeli, G., Karmann, B., Nance, J., Stigloher, C., & Wehman, A. M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1714085115 · Cited by 76
Distinct photo-oxidation-induced cell death pathways lead to selective killing of human breast cancer cells
dos Santos, A. F., Inague, A., Arini, G. S., Terra, L. F., Wailemann, R. A. M., Pimentel, A. C., Yoshinaga, M. Y., Silva, R., Severino, D., de Almeida, D. R. Q., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03275-2 · Cited by 73
Membrane Heterogeneity Controls Cellular Endocytic Trafficking
Redpath, G. M. I., Betzler, V. M., Rossatti, P., & Rossy, J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00757 · Cited by 66
Critical roles of phosphoinositides and NF2 in Hippo pathway regulationPreprint
Hong, A. W., Meng, Z., Plouffe, S. W., Lin, Z., Zhang, M., & Guan, K. (2020) · Genes & Development · doi:10.1101/gad.333435.119 · Cited by 66
A phosphoinositide switch mediates exocyst recruitment to multivesicular endosomes for exosome secretion
Liu, D.-A., Tao, K. X., Wu, B., Yu, Z., Szczepaniak, M., Rames, M. J., Yang, C., Svitkina, T., Zhu, Y., Xu, F., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42661-0 · Cited by 72
The expanding organelle lipidomes: current knowledge and challenges
Sarmento, M. J., Llorente, A., Petan, T., Khnykin, D., Popa, I., Perković, M. N., Konjevod, M., & Jaganjac, M. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04889-3 · Cited by 69
The Legionella pneumophila Dot/Icm type IV secretion system and its effectors
Lockwood, D. C., Amin, H., Costa, T. R. D., & Schroeder, G. N. (2022) · Microbiology · doi:10.1099/mic.0.001187 · Cited by 63
The signaling lipid phosphatidylinositol‐3,5‐bisphosphate targets plant CLC‐a anion/H+ exchange activity
Carpaneto, A., Boccaccio, A., Lagostena, L., Zanni, E. D., & Scholz‐Starke, J. (2017) · EMBO Reports · doi:10.15252/embr.201643814 · Cited by 56
Phosphoinositide lipids in primary cilia biology
Conduit, S. E., & Vanhaesebroeck, B. (2020) · Biochemical Journal · doi:10.1042/bcj20200277 · Cited by 56
Lipid kinases VPS34 and PIKfyve coordinate a phosphoinositide cascade to regulate retriever-mediated recycling on endosomes
Giridharan, S. S. P., Luo, G., Rivero-Rios, P., Steinfeld, N., Tronchere, H., Singla, A., Burstein, E., Billadeau, D. D., Sutton, M. A., & Weisman, L. S. (2022) · eLife · doi:10.7554/elife.69709 · Cited by 61
Phosphoinositides and the Fate of Legionella in Phagocytes
Swart, A. L., & Hilbi, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00025 · Cited by 52
Lipids and Lipid-Binding Proteins in Selective Autophagy
de la Ballina, L. R., Munson, M. J., & Simonsen, A. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.05.051 · Cited by 53
Phosphoinositide switches in endocytosis and in the endolysosomal system
Wang, H., Lo, W., & Haucke, V. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.03.011 · Cited by 54
Septin 9 has Two Polybasic Domains Critical to Septin Filament Assembly and Golgi Integrity
Omrane, M., Câmara, A. S., Taveneau, C., Benzoubir, N., Tubiana, T., Yu, J., Guérois, R., Samuel, D., Goud, B., Poüs, C., et al. (2019) · iScience · doi:10.1016/j.isci.2019.02.015 · Cited by 51
PLEKHA4/kramer Attenuates Dishevelled Ubiquitination to Modulate Wnt and Planar Cell Polarity Signaling
Shah, A. S., Batrouni, A. G., Kim, D.-S., Punyala, A., Cao, W., Han, C., Goldberg, M. L., Smolka, M. B., & Baskin, J. M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.060 · Cited by 46
Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins
Pemberton, J. G., & Balla, T. (2018) · Advances in experimental medicine and biology · doi:10.1007/5584_2018_288 · Cited by 46
Critical role for Piccolo in synaptic vesicle retrieval
Ackermann, F., Schink, K. O., Bruns, C., Izsvák, Z., Hamra, F. K., Rosenmund, C., & Garner, C. C. (2019) · eLife · doi:10.7554/elife.46629 · Cited by 46
Self-citation
Integrated regulation of the phosphatidylinositol cycle and phosphoinositide‐driven lipid transport at ER‐PM contact sites
Pemberton, J. G., Kim, Y. J., & Balla, T. (2019) · Traffic · doi:10.1111/tra.12709 · Cited by 44
Isomer Selective Comprehensive Lipidomics Analysis of Phosphoinositides in Biological Samples by Liquid Chromatography with Data Independent Acquisition Tandem Mass Spectrometry
Li, P., & Lämmerhofer, M. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c01751 · Cited by 46
Control of vacuole membrane homeostasis by a resident PI-3,5-kinase inhibitor
Malia, P. C., Numrich, J., Nishimura, T., Montoro, A. G., Stefan, C. J., & Ungermann, C. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722517115 · Cited by 45
A plant‐unique ESCRT component, FYVE4, regulates multivesicular endosome biogenesis and plant growth
Liu, C., Zeng, Y., Li, H., Yang, C., Shen, W., Xu, M., Xiao, Z., Chen, T., Li, B., Cao, W., et al. (2021) · New Phytologist · doi:10.1111/nph.17358 · Cited by 46
No longer married to inflammasome signaling: the diverse interacting pathways leading to pyroptotic cell death
Weir, A. L., & Vince, J. E. (2022) · Biochemical Journal · doi:10.1042/bcj20210711 · Cited by 45
Avidity‐driven polarity establishment via multivalent lipid–GTPase module interactions
Meca, J., Massoni‐Laporte, A., Sartorel, E., Martinez, D., Loquet, A., Habenstein, B., & McCusker, D. (2018) · The EMBO Journal · doi:10.15252/embj.201899652 · Cited by 43
Externalized phosphatidylinositides on apoptotic cells are eat-me signals recognized by CD14
Kim, O., Kang, G.-H., Hur, J., Lee, J. W., Jung, Y., Hong, I., Lee, H., Seo, S., Lee, D. H., Lee, C.-S., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00931-2 · Cited by 42
PI(4,5)P2 diffuses freely in the plasma membrane even within high-density effector protein complexes
Pacheco, J. E., Cassidy, A. C., Zewe, J. P., Wills, R. C., & Hammond, G. R. V. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202204099 · Cited by 44
Lipids that directly regulate innate immune signal transduction
Barnett, K. C., & Kagan, J. C. (2019) · Innate Immunity · doi:10.1177/1753425919852695 · Cited by 44
Lichen-like association of Chlamydomonas reinhardtii and Aspergillus nidulans protects algal cells from bacteria
Krespach, M. K. C., García‐Altares, M., Flak, M., Schoeler, H., Scherlach, K., Netzker, T., Schmalzl, A., Mattern, D. J., Schroeckh, V., Komor, A. J., et al. (2020) · The ISME Journal · doi:10.1038/s41396-020-0731-2 · Cited by 42
A Phosphoinositide-Binding Protein Acts in the Trafficking Pathway of Hemoglobin in the Malaria Parasite Plasmodium falciparum
Mukherjee, A., Crochetière, M., Sergerie, A., Amiar, S., Thompson, L. A., Ebrahimzadeh, Z., Gagnon, D., Lauruol, F., Bourgeois, A., Galaup, T., et al. (2022) · mBio · doi:10.1128/mbio.03239-21 · Cited by 37
Local detection of PtdIns3P at autophagosome biogenesis membrane platforms
Nascimbeni, A. C., Codogno, P., & Morel, É. (2017) · Autophagy · doi:10.1080/15548627.2017.1341465 · Cited by 45
Phosphatidylinositol Kinases and Phosphatases in Entamoeba histolytica
Nakada‐Tsukui, K., Watanabe, N., Maehama, T., & Nozaki, T. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00150 · Cited by 42
The where, what, and when of membrane protein degradation in neurons
Jin, E. J., Kiral, F. R., & Hiesinger, P. R. (2017) · Developmental Neurobiology · doi:10.1002/dneu.22534 · Cited by 38
Determinants of Peroxisome Membrane Dynamics
Carmichael, R. E., & Schrader, M. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.834411 · Cited by 39
De novo variation in bipolar disorder
Goes, F. S., Pirooznia, M., Tehan, M., Zandi, P. P., McGrath, J. A., Wolyniec, P. S., Nestadt, G., & Pulver, A. E. (2019) · Molecular Psychiatry · doi:10.1038/s41380-019-0611-1 · Cited by 37
Mechanisms behind the polarized distribution of lipids in epithelial cells
van IJzendoorn, S. C. D., Agnetti, J., & Gassama‐Diagne, A. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.183145 · Cited by 37
Legionella -Containing Vacuoles Capture PtdIns(4) P -Rich Vesicles Derived from the Golgi Apparatus
Weber, S., Steiner, B., Welin, A., & Hilbi, H. (2018) · mBio · doi:10.1128/mbio.02420-18 · Cited by 35
Phosphoinositide lipids in primary cilia biology
Conduit, S. E., & Vanhaesebroeck, B. (2020) · UCL Discovery (University College London) · Cited by 36
Differences in Granule Morphology yet Equally Impaired Exocytosis among Cytotoxic T Cells and NK Cells from Chediak–Higashi Syndrome Patients
Chiang, S. C. C., Wood, S. M., Tesi, B., Akar, H. H., Al–Herz, W., Ammann, S., Belen, F. B., Çalışkan, Ü., Kaya, Z., Lehmberg, K., et al. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00426 · Cited by 33
The autophagy protein ATG16L1 cooperates with IFT20 and INPP5E to regulate the turnover of phosphoinositides at the primary cilium
Boukhalfa, A., Roccio, F., Dupont, N., Codogno, P., & Morel, É. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109045 · Cited by 34
WDR81 regulates adult hippocampal neurogenesis through endosomal SARA-TGFβ signaling
Wang, M., Tang, C., Xing, R., Liu, X., Han, X. W., Liu, Y., Wang, L., Yang, C., & Guo, W. (2018) · Molecular Psychiatry · doi:10.1038/s41380-018-0307-y · Cited by 34
A conserved myotubularin-related phosphatase regulates autophagy by maintaining autophagic flux
Allen, E. A., Amato, C., Fortier, T. M., Velentzas, P. D., Wood, W., & Baehrecke, E. H. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201909073 · Cited by 32
Membrane-bound O-acyltransferase 7 (MBOAT7)-driven phosphatidylinositol remodeling in advanced liver disease
Varadharajan, V., Massey, W. J., & Brown, J. M. (2022) · Journal of Lipid Research · doi:10.1016/j.jlr.2022.100234 · Cited by 32
A novel homeostatic mechanism tunes PI(4,5)P2-dependent signaling at the plasma membrane
Wills, R. C., Doyle, C. P., Zewe, J. P., Pacheco, J. E., Hansen, S. D., & Hammond, G. R. V. (2023) · Journal of Cell Science · doi:10.1242/jcs.261494 · Cited by 34
Recombinant biosensors for multiplex and super-resolution imaging of phosphoinositides
Maib, H., Adarska, P., Hunton, R., Vines, J. H., Strutt, D. I., Bottanelli, F., & Murray, D. H. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202310095 · Cited by 31
Phosphoinositides in Retinal Function and Disease
Wensel, T. G. (2020) · Cells · doi:10.3390/cells9040866 · Cited by 32
Class II phosphatidylinositol 3-kinase isoforms in vesicular trafficking
Yoshioka, K. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200835 · Cited by 31
Phosphoinositide Signaling and Mechanotransduction in Cardiovascular Biology and Disease
Krajnik, A., Brazzo, J. A., Vaidyanathan, K., Das, T., Redondo-Muñóz, J., & Bae, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.595849 · Cited by 31
Metabolic routing maintains the unique fatty acid composition of phosphoinositides
Kim, Y. J., Sengupta, N., Sohn, M., Mandal, A., Pemberton, J. G., Choi, U., & Balla, T. (2022) · EMBO Reports · doi:10.15252/embr.202154532 · Cited by 30
Local synthesis of the phosphatidylinositol-3,4-bisphosphate lipid drives focal adhesion turnover
Posor, Y., Kampyli, C., Bilanges, B., Ganguli, S., Koch, P. A., Wallroth, A., Morelli, D., Jenkins, M., Alliouachene, S., Deltcheva, E. M., et al. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.06.011 · Cited by 30
Autophagy in the eye: from physiology to pathophysiology
Liton, P. B., Boesze‐Battaglia, K., Boulton, M. E., Boya, P., Ferguson, T. A., Ganley, I. G., Kauppinen, A., Laurie, G. W., Mizushima, N., Morishita, H., et al. (2023) · Autophagy Reports · doi:10.1080/27694127.2023.2178996 · Cited by 31
α-Synuclein-112 Impairs Synaptic Vesicle Recycling Consistent With Its Enhanced Membrane Binding Properties
Soll, L. G., Eisen, J. N., Vargas, K. J., Medeiros, A. T., Hammar, K. M., & Morgan, J. R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00405 · Cited by 29
A dynamic partitioning mechanism polarizes membrane protein distribution
Banerjee, T., Matsuoka, S., Biswas, D., Miao, Y., Pal, D. S., Kamimura, Y., Ueda, M., Devreotes, P. N., & Iglesias, P. A. (2023) · Nature Communications · doi:10.1038/s41467-023-43615-2 · Cited by 28
Schwann cell‐specific deletion of the endosomal PI 3‐kinase Vps34 leads to delayed radial sorting of axons, arrested myelination, and abnormal ErbB2‐ErbB3 tyrosine kinase signaling
Logan, A. M., Mammel, A. E., Robinson, D. C., Chin, A. L., Condon, A. F., & Robinson, F. L. (2017) · Glia · doi:10.1002/glia.23173 · Cited by 27
Helicobacter pylori CagA oncoprotein interacts with SHIP2 to increase its delivery into gastric epithelial cells
Fujii, Y., Murata‐Kamiya, N., & Hatakeyama, M. (2020) · Cancer Science · doi:10.1111/cas.14391 · Cited by 26
How neurons maintain their axons long-term: an integrated view of axon biology and pathology
Smith, G. A., Sweeney, S. T., O’Kane, C. J., & Prokop, A. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1236815 · Cited by 28
Recent advances in understanding phosphoinositide signaling in the nervous system
Dickson, E. J. (2019) · F1000Research · doi:10.12688/f1000research.16679.1 · Cited by 26
Taurine Attenuates Streptococcus uberis-Induced Bovine Mammary Epithelial Cells Inflammation via Phosphoinositides/Ca2+ Signaling
Li, M., Xi, P., Xu, Y., Wang, Z., Han, X., Ren, W., Phouthapane, V., & Miao, J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01825 · Cited by 25
An ARF GTPase module promoting invasion and metastasis through regulating phosphoinositide metabolism
Nacke, M., Sandilands, E., Nikolatou, K., Román‐Fernández, Á., Mason, S. M., Patel, R., Lilla, S., Yelland, T., Galbraith, L. C. A., Freckmann, E. C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21847-4 · Cited by 24
Phospholipids of the Plasma Membrane – Regulators or Consequence of Cell Polarity?
Krahn, M. P. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00277 · Cited by 26
Lipid asymmetry and membrane trafficking: Transbilayer distribution of structural phospholipids as regulators of exocytosis and endocytosis
Caputo, M., Gubar, O. S., Tóth, P., Vitale, N., Gasman, S., & Ory, S. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110441 · Cited by 25
The Intimate Connection Between Lipids and Hedgehog Signaling
Nguyen, T. D., Truong, M. E., & Reiter, J. F. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.876815 · Cited by 25
The intracellular Ca 2+ channel TRPML3 is a PI3P effector that regulates autophagosome biogenesis
Kim, S. W., Kim, M. K., Hong, S., Choi, A., Choi, J. H., Muallem, S., So, I., Yang, D., & Kim, H. J. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2200085119 · Cited by 24
Lipid-mediated activation of plasma membrane-localized deubiquitylating enzymes modulate endosomal trafficking
Vogel, K., Bläske, T., Nagel, M.-K., Globisch, C., Maguire, S., Mattes, L., Gude, C., Kovermann, M., Hauser, K., Peter, C., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34637-3 · Cited by 24
Lipid Biomarkers in Liquid Biopsies: Novel Opportunities for Cancer Diagnosis
Sagini, K., Urbanelli, L., Buratta, S., Emiliani, C., & Llorente, A. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15020437 · Cited by 30
The class III phosphatidylinositol 3-kinase Vps34 in Saccharomyces cerevisiae
Reidick, C., Boutouja, F., & Platta, H. W. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0288 · Cited by 27
The Many Roles of Type II Phosphatidylinositol 4‐Kinases in Membrane Trafficking: New Tricks for Old Dogs
Minogue, S. (2017) · BioEssays · doi:10.1002/bies.201700145 · Cited by 25
Definition of phosphoinositide distribution in the nanoscale
Tsuji, T., Takatori, S., & Fujimoto, T. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.10.008 · Cited by 25
Divalent cations bind to phosphoinositides to induce ion and isomer specific propensities for nano-cluster initiation in bilayer membranes
Bradley, R. P., Slochower, D. R., Janmey, P. A., & Radhakrishnan, R. (2020) · Royal Society Open Science · doi:10.1098/rsos.192208 · Cited by 25

Authors: Schink, K. O., Tan, K.-W., & Stenmark, H.
Affiliations: Oslo University Hospital (NO)
ORCID: Schink, Kay O.
Tan, Kia-Wee
Stenmark, Harald
Venue: Annual Review of Cell and Developmental Biology
Publisher: Annual Reviews
Published: 2016-10-06
Volume: 32
Issue: 1
Pages: 143-171
ISSN: 1081-0706 (ISSN-L)
1530-8995
DOI: 10.1146/annurev-cellbio-111315-125349
OpenAlex: W2311826957
Cited by: 283
References: 158
Citations by year: 2026: 14 · 2025: 19 · 2024: 23 · 2023: 32 · 2022: 39 · 2021: 25 · 2020: 45 · 2019: 40 · 2018: 25 · 2017: 16 · 2016: 5
FWCI: 3.10
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Cell and Developmental Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords: phosphoinositides, membrane dynamics, phosphatidylinositol, membrane recruitment, membrane fusion, exocytosis, endocytosis, autophagy, cell division, cell migration, epithelial polarity
MeSH terms: Animals, Autophagy, Cell Membrane, Endocytosis, Epithelial Cells, Exocytosis, Humans, Phosphatidylinositols

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Phosphoinositides in Control of Membrane Dynamics

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks