Cited by 387Calcium signaling and nucleotide metabolismCellular transport and secretionAutophagy in Disease and Therapy

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A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation

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Li, Xinran, Rydzewski, Nicholas, Hider, Ahmad, Zhang, Xiaoli, Yang, Junsheng, Wang, Wuyang, Gao, Qiong, Cheng, Xiping, Xu, Haoxing·2016·Nature Cell Biology

DOI 10.1038/ncb3324PMC PMC4871318

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Abstract

To mediate the degradation of biomacromolecules, lysosomes must traffic towards cargo-carrying vesicles for subsequent membrane fusion or fission. Mutations of the lysosomal Ca(2+) channel TRPML1 cause lysosomal storage disease (LSD) characterized by disordered lysosomal membrane trafficking in cells. Here we show that TRPML1 activity is required to promote Ca(2+)-dependent centripetal movement of lysosomes towards the perinuclear region (where autophagosomes accumulate) following autophagy induction. ALG-2, an EF-hand-containing protein, serves as a lysosomal Ca(2+) sensor that associates physically with the minus-end-directed dynactin-dynein motor, while PtdIns(3,5)P(2), a lysosome-localized phosphoinositide, acts upstream of TRPML1. Furthermore, the PtdIns(3,5)P(2)-TRPML1-ALG-2-dynein signalling is necessary for lysosome tubulation and reformation. In contrast, the TRPML1 pathway is not required for the perinuclear accumulation of lysosomes observed in many LSDs, which is instead likely to be caused by secondary cholesterol accumulation that constitutively activates Rab7-RILP-dependent retrograde transport. Ca(2+) release from lysosomes thus provides an on-demand mechanism regulating lysosome motility, positioning and tubulation.

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AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
Ragulator-Rag Complex Targets mTORC1 to the Lysosomal Surface and Is Necessary for Its Activation by Amino Acids
Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464
Dissection of the Autophagosome Maturation Process by a Novel Reporter Protein, Tandem Fluorescent-Tagged LC3
Kimura, S., Noda, T., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4451 · Cited by 2,278
New calcium indicators and buffers with high selectivity against magnesium and protons: design, synthesis, and properties of prototype structures
Tsien, R. Y. (1980) · Biochemistry · doi:10.1021/bi00552a018 · Cited by 2,261
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
A ubiquitin-like system mediates protein lipidation
Ichimura, Y., Kirisako, T., Takao, T., Satomi, Y., Shimonishi, Y., Ishihara, N., Mizushima, N., Tanida, I., Kominami, E., Ohsumi, M., et al. (2000) · Nature · doi:10.1038/35044114 · Cited by 2,139
Lysosomes: fusion and function
Luzio, J. P., Pryor, P. R., & Bright, N. A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2217 · Cited by 1,807
An ATP-competitive Mammalian Target of Rapamycin Inhibitor Reveals Rapamycin-resistant Functions of mTORC1
Thoreen, C. C., Kang, S. A., Chang, J. W., Liu, Q., Zhang, J., Gao, Y., Reichling, L. J., Sim, T., Sabatini, D. M., & Gray, N. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900301200 · Cited by 1,803
Kinesin and Dynein Superfamily Proteins and the Mechanism of Organelle Transport
Hirokawa, N. (1998) · Science · doi:10.1126/science.279.5350.519 · Cited by 1,689
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H + -ATPase
Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M. (2011) · Science · doi:10.1126/science.1207056 · Cited by 1,673
Termination of autophagy and reformation of lysosomes regulated by mTOR
Yu, L., McPhee, C. K., Zheng, L., Mardones, G. A., Rong, Y., Peng, J., Mi, N., Zhao, Y., Liu, Z., Wan, F., et al. (2010) · Nature · doi:10.1038/nature09076 · Cited by 1,544
Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB
Medina, D. L., Paola, S. D., Peluso, I., Armani, A., Stefani, D. D., Venditti, R., Montefusco, S., Rosato, A. S., Prezioso, C., Forrester, A. R., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3114 · Cited by 1,452
Self-citation
Membrane recognition by phospholipid-binding domains
Lemmon, M. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2328 · Cited by 1,419
Transient Receptor Potential Cation Channels in Disease
Nilius, B., Owsianik, G., Voets, T., & Peters, J. A. (2007) · Physiological Reviews · doi:10.1152/physrev.00021.2006 · Cited by 1,419
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
Rab7: A Key to Lysosome Biogenesis
Bucci, C., Thomsen, P., Nicoziani, P., McCarthy, J., & van Deurs, B. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.2.467 · Cited by 1,108
Lysosomal Physiology
Xu, H., & Ren, D. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021014-071649 · Cited by 1,067
Self-citation
Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
Gillooly, D. J., Morrow, I. C., Lindsay, M., Gould, R., Bryant, N. J., Gaullier, J., Parton, R. G., & Stenmark, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4577 · Cited by 1,031
Caveolae as plasma membrane sensors, protectors and organizers
Parton, R. G., & del Pozo, M. Á. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3512 · Cited by 984
Chaperone-mediated autophagy: a unique way to enter the lysosome world
Kaushik, S., & Cuervo, A. M. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.05.006 · Cited by 905
Lysosomal positioning coordinates cellular nutrient responses
Korolchuk, V. I., Saiki, S., Lichtenberg, M., Siddiqi, F. H., Roberts, E. A., Imarisio, S., Jahreiss, L., Sarkar, S., Futter, M., Menzies, F. M., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2204 · Cited by 891
Visualization of Phosphoinositides That Bind Pleckstrin Homology Domains: Calcium- and Agonist-induced Dynamic Changes and Relationship to Myo-[3H]inositol-labeled Phosphoinositide Pools
Várnai, P., & Balla, T. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.501 · Cited by 859
Bafilomycin A1 disrupts autophagic flux by inhibiting both V-ATPase-dependent acidification and Ca-P60A/SERCA-dependent autophagosome-lysosome fusion
Mauvezin, C., & Neufeld, T. P. (2015) · Autophagy · doi:10.1080/15548627.2015.1066957 · Cited by 817
Sorting of lysosomal proteins
Braulke, T., & Bonifacino, J. S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.10.016 · Cited by 811
The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors
Jordens, I., Fernandez-Borja, M., Marsman, M., Dusseljee, S., Janssen, L., Calafat, J., Janssen, H., Wubbolts, R., & Neefjes, J. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00531-0 · Cited by 811
Spatial Control of the TSC Complex Integrates Insulin and Nutrient Regulation of mTORC1 at the Lysosome
Menon, S., Dibble, C. C., Talbott, G., Hoxhaj, G., Valvezan, A. J., Takahashi, H., Cantley, L. C., & Manning, B. D. (2014) · Cell · doi:10.1016/j.cell.2013.11.049 · Cited by 766
Macropinocytosis: an endocytic pathway for internalising large gulps
Lim, J. P., & Gleeson, P. A. (2011) · Immunology and Cell Biology · doi:10.1038/icb.2011.20 · Cited by 705
Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7–RILP–p150Glued and late endosome positioning
Rocha, N., Kuijl, C. P., van der Kant, R., Janssen, L., Houben, D., Janssen, H., Zwart, W. T., & Neefjes, J. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200811005 · Cited by 705
Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles.
Pearse, B. M. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.4.1255 · Cited by 683
Overexpression of the Dynamitin (p50) Subunit of the Dynactin Complex Disrupts Dynein-dependent Maintenance of Membrane Organelle Distribution
Burkhardt, J. K., Echeverri, C. J., Nilsson, T., & Vallee, R. B. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.2.469 · Cited by 667
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
Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria
Tanaka, Y., Kanai, Y., Okada, Y., Nonaka, S., Takeda, S., Harada, A., & Hirokawa, N. (1998) · Cell · doi:10.1016/s0092-8674(00)81459-2 · Cited by 654
PI(3,5)P2 controls membrane trafficking by direct activation of mucolipin Ca2+ release channels in the endolysosome
Dong, X., Shen, D., Wang, X., Dawson, T., Li, X., Zhang, Q., Cheng, X., Zhang, Y., Weisman, L. S., Delling, M., et al. (2010) · Nature Communications · doi:10.1038/ncomms1037 · Cited by 645
Self-citation
DYNACTIN
Schroer, T. A. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.012103.094623 · Cited by 614
The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
Dong, X., Cheng, X., Mills, E., Delling, M., Wang, F., Kurz, T., & Xu, H. (2008) · Nature · doi:10.1038/nature07311 · Cited by 588
Self-citation
Traffic control: regulation of kinesin motors
Verhey, K. J., & Hammond, J. W. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2782 · Cited by 546
TPC Proteins Are Phosphoinositide- Activated Sodium-Selective Ion Channels in Endosomes and Lysosomes
Wang, X., Zhang, X., Dong, X., Samie, M., Li, X., Cheng, X., Goschka, A., Shen, D., Zhou, Y., Harlow, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.08.036 · Cited by 545
Self-citation
Genome Engineering Using CRISPR-Cas9 System
Cong, L., & Zhang, F. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-1862-1_10 · Cited by 536
Mitochondrial Trafficking in Neurons
Schwarz, T. L. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011304 · Cited by 525
GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
Roux, A., Uyhazi, K., Frost, A., & Camilli, P. D. (2006) · Nature · doi:10.1038/nature04718 · Cited by 524
Activation of endosomal dynein motors by stepwise assembly of Rab7–RILP–p150Glued, ORP1L, and the receptor βlll spectrin
Johansson, M., Rocha, N., Zwart, W., Jordens, I., Janssen, L., Kuijl, C., Olkkonen, V. M., & Neefjes, J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606077 · Cited by 505
Lipid storage disorders block lysosomal trafficking by inhibiting a TRP channel and lysosomal calcium release
Shen, D., Wang, X., Li, X., Zhang, X., Yao, Z., Dibble, S., Dong, X., Yu, T., Lieberman, A. P., Showalter, H. D., et al. (2012) · Nature Communications · doi:10.1038/ncomms1735 · Cited by 497
Self-citation
A novel fluorescent ceramide analogue for studying membrane traffic in animal cells: accumulation at the Golgi apparatus results in altered spectral properties of the sphingolipid precursor.
Pagano, R. E., Martin, O. C., Kang, H. C., & Haugland, R. P. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.113.6.1267 · Cited by 491
Rab‐interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes
Cantalupo, G., Alifano, P., Roberti, V., Bruni, C. B., & Bucci, C. (2001) · The EMBO Journal · doi:10.1093/emboj/20.4.683 · Cited by 488
Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel
Sun, M. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.17.2471 · Cited by 461
Dynein-dependent Movement of Autophagosomes Mediates Efficient Encounters with Lysosomes
Kimura, S., Noda, T., & Yoshimori, T. (2008) · Cell Structure and Function · doi:10.1247/csf.08005 · Cited by 438
Vacuolar and Plasma Membrane Proton-Adenosinetriphosphatases
Nelson, N., & Harvey, W. R. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.2.361 · Cited by 420
Identification of the gene causing mucolipidosis type IV
Bargal, R., Avidan, N., Ben‐Asher, E., Olender, Z., Zeigler, M., Frumkin, A., Raas‐Rothschild, A., Glusman, G., Lancet, D., & Bach, G. (2000) · Nature Genetics · doi:10.1038/79095 · Cited by 406
The Ras protein superfamily: Evolutionary tree and role of conserved amino acids
Rojas, A. M., Fuentes, G., Rausell, A., & Valencia, A. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201103008 · Cited by 406
Endosomal sorting and signalling: an emerging role for sorting nexins
Cullen, P. J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2427 · Cited by 404
Small-molecule inhibitors of the AAA+ ATPase motor cytoplasmic dynein
Firestone, A. J., Weinger, J. S., Maldonado, M., Barlan, K., Langston, L. D., O’Donnell, M., Gelfand, V. I., Kapoor, T. M., & Chen, J. K. (2012) · Nature · doi:10.1038/nature10936 · Cited by 403
MVB vesicle formation: ESCRT-dependent, ESCRT-independent and everything in between
Babst, M. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.04.008 · Cited by 399
Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion
Peters, C., & Mayer, A. (1998) · Nature · doi:10.1038/25133 · Cited by 386
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
Mechanism of Ca2+-triggered ESCRT assembly and regulation of cell membrane repair
Scheffer, L., Sreetama, S. C., Sharma, N., Medikayala, S., Brown, K. J., Defour, A., & Jaiswal, J. K. (2014) · Nature Communications · doi:10.1038/ncomms6646 · Cited by 372
GTPase Networks in Membrane Traffic
Mizuno-Yamasaki, E., Rivera-Molina, F. E., & Novick, P. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052810-093700 · Cited by 366
Arl8 and SKIP Act Together to Link Lysosomes to Kinesin-1
Rosa-Ferreira, C., & Munro, S. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.10.007 · Cited by 360
The dynein microtubule motor
King, S. M. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00009-4 · Cited by 338
Tethering Factors as Organizers of Intracellular Vesicular Traffic
Yu, I.-M., & Hughson, F. M. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.042308.113327 · Cited by 330
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
Self-citation
A selective PIKfyve inhibitor blocks PtdIns(3,5)P2 production and disrupts endomembrane transport and retroviral budding
Jefferies, H. B. J., Cooke, F. T., Jat, P., Boucheron, C., Koizumi, T., Hayakawa, M., Kaizawa, H., Ohishi, T., Workman, P., Waterfield, M. D., et al. (2008) · EMBO Reports · doi:10.1038/sj.embor.7401155 · Cited by 305
Clathrin and phosphatidylinositol-4,5-bisphosphate regulate autophagic lysosome reformation
Rong, Y., Liu, M., Ma, L., Du, W., Zhang, H., Tian, Y., Cao, Z., Li, Y., Ren, H., Zhang, C., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2557 · Cited by 297
Membrane Fusion: Five Lipids, Four SNAREs, Three Chaperones, Two Nucleotides, and a Rab, All Dancing in a Ring on Yeast Vacuoles
Wickner, W. T. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104131 · Cited by 280
Tubular lysosome morphology and distribution within macrophages depend on the integrity of cytoplasmic microtubules.
Swanson, J. A., Bushnell, A. F., & Silverstein, S. C. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.7.1921 · Cited by 274
Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation
Rong, Y., McPhee, C. K., Deng, S., Huang, L., Chen, L., Liu, M., Tracy, K., Baehrecke, E. H., Yu, L., & Lenardo, M. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013800108 · Cited by 273
Mucolipins: Intracellular TRPML1‐3 channels
Cheng, X., Shen, D., Samie, M., & Xu, H. (2010) · FEBS Letters · doi:10.1016/j.febslet.2009.12.056 · Cited by 272
Self-citation
VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P2 in yeast and mouse
Jin, N., Chow, C. Y., Liu, L., Zolov, S. N., Bronson, R. T., Davisson, M. T., Petersen, J. L., Zhang, Y., Park, S., Duex, J. E., et al. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.248 · Cited by 266
Cloning of the Gene Encoding a Novel Integral Membrane Protein, Mucolipidin—and Identification of the Two Major Founder Mutations Causing Mucolipidosis Type IV
Bassi, M. T., Manzoni, M., Monti, E., Pizzo, M. T., Ballabio, A., & Borsani, G. (2000) · The American Journal of Human Genetics · doi:10.1016/s0002-9297(07)62941-3 · Cited by 260
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
Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation
Wang, W., Gao, Q., Yang, M., Zhang, X., Yu, L., Lawas, M., Li, X., Bryant-Genevier, M. G., Southall, N. T., Marugán, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419669112 · Cited by 247
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
TRP-ML1 Regulates Lysosomal pH and Acidic Lysosomal Lipid Hydrolytic Activity
Soyombo, A. A., Tjon‐Kon‐Sang, S., Rbaibi, Y., Bashllari, E., Bisceglia, J., Muallem, S., & Kiselyov, K. I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508211200 · Cited by 235
Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation
Chang, J., Lee, S., & Blackstone, C. D. (2014) · Journal of Clinical Investigation · doi:10.1172/jci77598 · Cited by 224
The Vps35 D620N Mutation Linked to Parkinson's Disease Disrupts the Cargo Sorting Function of Retromer
Follett, J., Norwood, S. J., Hamilton, N., Mohan, M., Kovtun, O., Tay, S. V., Yang, Z., Wood, S. A., Mellick, G. D., Silburn, P. A., et al. (2013) · Traffic · doi:10.1111/tra.12136 · Cited by 223
Linking molecular motors to membrane cargo
Akhmanova, A. S., & Hammer, J. A. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.04.008 · Cited by 218
PIKfyve, a Class III PI Kinase, Is the Target of the Small Molecular IL-12/IL-23 Inhibitor Apilimod and a Player in Toll-like Receptor Signaling
Cai, X., Xu, Y., Cheung, A. K., Tomlinson, R., Alcázar-Román, A. R., Murphy, L. O., Billich, A., Zhang, B., Feng, Y., Klumpp, M., et al. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.05.010 · Cited by 214
Phosphatidylinositol 3,5-bisphosphate and Fab1p/PIKfyve underPPIn endo-lysosome function
Dove, S. K., Dong, K., Kobayashi, T., Williams, F. K., & Michell, R. H. (2009) · Biochemical Journal · doi:10.1042/bj20081950 · Cited by 208
Late endosomal transport and tethering are coupled processes controlled by RILP and the cholesterol sensor ORP1L
van der Kant, R., Fish, A., Janssen, L., Janssen, H., Schipper-Krom, S., Ho, N. I., Brummelkamp, T. R., Carette, J. E., Rocha, N., & Neefjes, J. (2013) · Journal of Cell Science · doi:10.1242/jcs.129270 · Cited by 205
Abnormal transport along the lysosomal pathway in Mucolipidosis, type IV disease
Chen, C.-S., Bach, G., & Pagano, R. E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6373 · Cited by 204
Direct mobilisation of lysosomal Ca2+ triggers complex Ca2+ signals
Kilpatrick, B. S., Eden, E. R., Schapira, A. H. V., Futter, C. E., & Patel, S. (2012) · Journal of Cell Science · doi:10.1242/jcs.118836 · Cited by 195
Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells
Navone, F., Niclas, J., Hom-Booher, N., Sparks, L. L., Bernstein, H., McCaffrey, G., & Vale, R. D. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.117.6.1263 · Cited by 194
Localization of Rheb to the endomembrane is critical for its signaling function
Buerger, C., DeVries, B., & Stambolic, V. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.220 · Cited by 192
Tethering complexes in the endocytic pathway: CORVET and HOPS
Solinger, J. A., & Spang, A. (2013) · FEBS Journal · doi:10.1111/febs.12151 · Cited by 192
Lysosomal exocytosis and lipid storage disorders
Samie, M. A., & Xu, H. (2014) · Journal of Lipid Research · doi:10.1194/jlr.r046896 · Cited by 192
Self-citation
Autophagic dysfunction in mucolipidosis type IV patients
Vergarajauregui, S., Connelly, P. S., Daniels, M. P., & Puertollano, R. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn174 · Cited by 182
Analysis of the Dynein-Dynactin Interaction In Vitro and In Vivo
King, S. J., Brown, C. L., Maier, K. C., Quintyne, N. J., & Schroer, T. A. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-01-0025 · Cited by 181
Directional Switching of the Kinesin Cin8 Through Motor Coupling
Roostalu, J., Hentrich, C., Bieling, P., Telley, I. A., Schiebel, E., & Surrey, T. (2011) · Science · doi:10.1126/science.1199945 · Cited by 180
Functional Characterization of Rab7 Mutant Proteins Associated with Charcot-Marie-Tooth Type 2B Disease
Spinosa, M. R., Progida, C., Luca, A. D., Colucci, A. M. R., Alifano, P., & Bucci, C. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3677-07.2008 · Cited by 176
Functional Characterization of Two Novel Mammalian Electrogenic Proton-dependent Amino Acid Cotransporters
Boll, M., Foltz, M., Rubio‐Aliaga, I., Kottra, G., & Daniel, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200374200 · Cited by 168
Phosphoinositide isoforms determine compartment-specific ion channel activity
Zhang, X., Li, X., & Xu, H. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202194109 · Cited by 167
Self-citation
Ca2+ and synaptotagmin VII–dependent delivery of lysosomal membrane to nascent phagosomes
Czibener, C., Sherer, N. M., Becker, S. M., Pypaert, M., Hui, E., Chapman, E. R., Mothes, W., & Andrews, N. W. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605004 · Cited by 165
Identification of Mammalian Vps24p as an Effector of Phosphatidylinositol 3,5-Bisphosphate-dependent Endosome Compartmentalization
Whitley, P. R., Reaves, B. J., Hashimoto, M., Riley, A. M., Potter, B. V. L., & Holman, G. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306864200 · Cited by 160
The Phosphoinositide Kinase PIKfyve Is Vital in Early Embryonic Development
Ikonomov, O. C., Sbrissa, D., Delvecchio, K., Xie, Y., Jin, J.-P., Rappolee, D., & Shisheva, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.222364 · Cited by 160
The C2 domains of synaptotagmin – partners in exocytosis
Bai, J. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.01.008 · Cited by 158
Mucolipin‐1 Is a Lysosomal Membrane Protein Required for Intracellular Lactosylceramide Traffic
Pryor, P. R., Reimann, F. M., Gribble, F. M., & Luzio, J. P. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00475.x · Cited by 156
Genetically encoded fluorescent probe to visualize intracellular phosphatidylinositol 3,5-bisphosphate localization and dynamics
Li, X., Wang, X., Zhang, X., Zhao, M., Tsang, W. L., Zhang, Y., Yau, R. G., Weisman, L. S., & Xu, H. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311864110 · Cited by 151
Self-citation
Visualizing Cellular Phosphoinositide Pools with GFP-Fused Protein-Modules
Balla, T., & Várnai, P. (2002) · Science s STKE · doi:10.1126/stke.2002.125.pl3 · Cited by 147
Cytoplasmic dynein heavy chain: the servant of many masters
Schiavo, G., Greensmith, L., Hafezparast, M., & Fisher, E. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.08.001 · Cited by 146
Acid sphingomyelinase, cell membranes and human disease: Lessons from Niemann–Pick disease
Schuchman, E. H. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.11.083 · Cited by 146
Neurologic, Gastric, and Opthalmologic Pathologies in a Murine Model of Mucolipidosis Type IV
Venugopal, B., Browning, M. F., Curcio‐Morelli, C., Varró, A., Michaud, N. A., Nanthakumar, N. N., Walkley, S. U., Pickel, J. M., & Slaugenhaupt, S. A. (2007) · The American Journal of Human Genetics · doi:10.1086/521954 · Cited by 146
Phosphatidylinositol 3,5-bisphosphate plays a role in the activation and subcellular localization of mechanistic target of rapamycin 1
Bridges, D., Ma, J.-T., Park, S., Inoki, K., Weisman, L. S., & Saltiel, A. R. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-12-1034 · Cited by 143
Lysosomes shape Ins(1,4,5)P3-evoked Ca2+ signals by selectively sequestering Ca2+ released from the endoplasmic reticulum
López-Sanjurjo, C. I., Tovey, S. C., Prole, D. L., & Taylor, C. W. (2012) · Journal of Cell Science · doi:10.1242/jcs.116103 · Cited by 138
Rab7 and Arl8 GTPases are Necessary for Lysosome Tubulation in Macrophages
Mrakovic, A., Kay, J. G., Furuya, W., Brumell, J. H., & Botelho, R. J. (2012) · Traffic · doi:10.1111/tra.12003 · Cited by 131
HOPS Proofreads thetrans-SNARE Complex for Yeast Vacuole Fusion
Starai, V. J., Hickey, C. M., & Wickner, W. T. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-01-0077 · Cited by 117
Membrane-trafficking sorting hubs: cooperation between PI4P and small GTPases at the trans-Golgi network
Santiago-Tirado, F. H., & Bretscher, A. P. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.05.005 · Cited by 116
Autophagic lysosome reformation
Chen, Y., & Yu, L. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.09.004 · Cited by 116
The intracellular Ca2+ channel MCOLN1 is required for sarcolemma repair to prevent muscular dystrophy
Cheng, X., Zhang, X., Gao, Q., Samie, M. A., Azar, M., Tsang, W. L., Dong, L., Sahoo, N., Li, X., Yue, Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3611 · Cited by 115
Self-citation
Drosophila TRPML Is Required for TORC1 Activation
Wong, C., Li, R., Montell, C., & Venkatachalam, K. (2012) · Current Biology · doi:10.1016/j.cub.2012.06.055 · Cited by 115
Membrane Traffic in Sphingolipid Storage Diseases
Pagano, R. E., Puri, V., Dominguez, M., & Marks, D. L. (2000) · Traffic · doi:10.1034/j.1600-0854.2000.011101.x · Cited by 111
Macroautophagy is defective in mucolipin-1-deficient mouse neurons
Curcio‐Morelli, C., Charles, F. A., Micsenyi, M. C., Cao, Y., Venugopal, B., Browning, M. F., Dobrenis, K., Cotman, S. L., Walkley, S. U., & Slaugenhaupt, S. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.06.010 · Cited by 110
Synaptotagmin-mediated vesicle fusion regulates cell migration
Colvin, R. A., Means, T. K., Diefenbach, T. J., Moita, L. F., Friday, R. P., Sever, S., Campanella, G. S. V., Abrazinski, T. A., Manice, L. A., Moita, C. F., et al. (2010) · Nature Immunology · doi:10.1038/ni.1878 · Cited by 108
The Phosphoinositide‐Gated Lysosomal Ca2+ Channel, TRPML1, Is Required for Phagosome Maturation
Dayam, R. M., Sarić, A., Shilliday, R. E., & Botelho, R. J. (2015) · Traffic · doi:10.1111/tra.12303 · Cited by 107
Zinc Dyshomeostasis Is Linked with the Loss of Mucolipidosis IV-associated TRPML1 Ion Channel
Eichelsdoerfer, J. L., Evans, J. A., Slaugenhaupt, S. A., & Cuajungco, M. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.165480 · Cited by 103
The Enlarged Lysosomes in beigej Cells Result From Decreased Lysosome Fission and Not Increased Lysosome Fusion
Durchfort, N., Verhoef, S., Vaughn, M. B., Shrestha, R., Adam, D., Kaplan, J., & Ward, D. M. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01300.x · Cited by 103
Inhibition of PIKfyve by YM-201636 Dysregulates Autophagy and Leads to Apoptosis-Independent Neuronal Cell Death
Martin, S., Harper, C. B., May, L. M., Coulson, E. J., Meunier, F. A., & Osborne, S. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060152 · Cited by 93
Recruitment of dynein to late endosomes and lysosomes through light intermediate chains
Tan, S. C., Scherer, J., & Vallee, R. B. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-02-0129 · Cited by 89
PI(3,5)P2 controls endosomal branched actin dynamics by regulating cortactin–actin interactions
Hong, N. H., Qi, A., & Weaver, A. M. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201412127 · Cited by 89
Identification of the Penta-EF-hand Protein ALG-2 as a Ca2+-dependent Interactor of Mucolipin-1
Vergarajauregui, S., Martina, J. A., & Puertollano, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.047241 · Cited by 85
trans-SNARE complex assembly and yeast vacuole membrane fusion
Collins, K. M., & Wickner, W. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702290104 · Cited by 83
Imaging phosphoinositide dynamics using GFP‐tagged protein domains
Halet, G. (2005) · Biology of the Cell · doi:10.1042/bc20040080 · Cited by 82
The dynein inhibitor C iliobrevin D inhibits the bidirectional transport of organelles along sensory axons and impairs NGF‐mediated regulation of growth cones and axon branches
Sainath, R., & Gallo, G. (2014) · Developmental Neurobiology · doi:10.1002/dneu.22246 · Cited by 81
Cholesterol Level Regulates Endosome Motility via Rab Proteins
Chen, H., Yang, J., Low, P. S., & Cheng, J. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.099366 · Cited by 80
Self-citation
ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner
Shibata, H., SUZUKI, H., Yoshida, H., & Maki, M. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.12.101 · Cited by 80
There's more to life than neurotransmission: the regulation of exocytosis by synaptotagmin VII
Andrews, N. W., & Chakrabarti, S. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.09.001 · Cited by 79
Regulation of intracellular pH by human peripheral blood lymphocytes as measured by 19F NMR.
DEUTSCH, C. J., Taylor, J. S., & Wilson, D. F. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.24.7944 · Cited by 78
Phosphatidylinositol metabolism and membrane fusion
Poccia, D., & Larijani, B. (2009) · Biochemical Journal · doi:10.1042/bj20082105 · Cited by 77
The mucolipidosis IV Ca2+ channel TRPML1 (MCOLN1) is regulated by the TOR kinase
Onyenwoke, R. U., Sexton, J. Z., Yan, F., Díaz, M. C. H., Forsberg, L. J., Major, M. B., & Brenman, J. E. (2015) · Biochemical Journal · doi:10.1042/bj20150219 · Cited by 77
Altered lysosomal positioning affects lysosomal functions in a cellular model of Huntington's disease
Erie, C., Sacino, M. F., Houle, L., Lu, M. L., & Wei, J. (2015) · European Journal of Neuroscience · doi:10.1111/ejn.12957 · Cited by 71
YM201636, an inhibitor of retroviral budding and PIKfyve-catalyzed PtdIns(3,5)P2 synthesis, halts glucose entry by insulin in adipocytes
Ikonomov, O., Sbrissa, D., & Shisheva, A. (2009) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2009.03.063 · Cited by 67
Structure and function of ALG-2, a penta-EF-hand calcium-dependent adaptor protein
Maki, M., SUZUKI, H., & Shibata, H. (2011) · Science China Life Sciences · doi:10.1007/s11427-011-4204-8 · Cited by 65
Cathepsin E Deficiency Induces a Novel Form of Lysosomal Storage Disorder Showing the Accumulation of Lysosomal Membrane Sialoglycoproteins and the Elevation of Lysosomal pH in Macrophages
Yanagawa, M., Tsukuba, T., Nishioku, T., Okamoto, Y., Okamoto, K., Takii, R., Terada, Y., Nakayama, K. I., Kadowaki, T., & Yamamoto, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604143200 · Cited by 60
Participation of dynamin in the biogenesis of cytoplasmic vesicles
Henley, J. R., Cao, H., & McNiven, M. A. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.9002.s243 · Cited by 60
Membrane Cholesterol Removal Changes Mechanical Properties of Cells and Induces Secretion of a Specific Pool of Lysosomes
Hissa, B., Pontes, B., Roma, P. M. D. S., Alves, A. P., Rocha, C. D., Valverde, T. M., de Aguiar, P. H. N., de Almeida, F. P., Guimaraes, A. J., Guatimosim, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082988 · Cited by 59
Modulation of synaptic function by VAC14, a protein that regulates the phosphoinositides PI(3,5)P2 and PI(5)P
Zhang, Y., McCartney, A. J., Zolov, S. N., Ferguson, C., Meisler, M. H., Sutton, M. A., & Weisman, L. S. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.200 · 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
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Trafficking defects in endogenously synthesized cholesterol in fibroblasts, macrophages, hepatocytes, and glial cells from Niemann-Pick type C1 mice
Reid, P., Sugii, S., & Chang, T. (2003) · Journal of Lipid Research · doi:10.1194/jlr.m300009-jlr200 · Cited by 51
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Helm, J. R., Bentley, M., Thorsen, K. D., Wang, T., Foltz, L., Oorschot, V. M. J., Klumperman, J., & Hay, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.561829 · Cited by 46
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Miller, A., Schafer, J., Upchurch, C. P., Spooner, E., Huynh, J. M., Hernandez, S., McLaughlin, B. M., Oden, L., & Fares, H. (2014) · Traffic · doi:10.1111/tra.12249 · Cited by 42
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Authors: Li, X., Rydzewski, N., Hider, A., Zhang, X., Yang, J., Wang, W., Gao, Q., Cheng, X., & Xu, H.
Affiliations: University of Michigan (US)
Zhejiang University of Technology (CN)
Corresponding author: Xu, Haoxing
ORCID: Li, Xinran
Rydzewski, Nicholas
Hider, Ahmad
Zhang, Xiaoli
Yang, Junsheng
Wang, Wuyang
Gao, Qiong
Cheng, Xiping
Xu, Haoxing
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2016-03-07
Volume: 18
Issue: 4
Pages: 404-417
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/ncb3324
PMC: PMC4871318
OpenAlex: W2299614729
Cited by: 387
References: 146
Citations by year: 2026: 26 · 2025: 25 · 2024: 38 · 2023: 36 · 2022: 46 · 2021: 44 · 2020: 42 · 2019: 30 · 2018: 44 · 2017: 39 · 2016: 17
FWCI: 39.52
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Deep Blue (University of Michigan) (submittedVersion)
Funders: National Institute of Mental Health (MH096595, R03MH096595)
National Institute of Neurological Disorders and Stroke (R21NS091928, NS062792, R01NS062792)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR060837, R01AR060837)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: lysosome motility, lysosome positioning, TRPML1, lysosomal storage disease, ALG-2, PtdIns(3,5)P2, autophagy, lysosomal calcium release, retrograde transport, cholesterol accumulation, perinuclear accumulation
MeSH terms: rab7 GTP-Binding Proteins, Animals, Autophagy, Base Sequence, Calcium, Calcium-Binding Proteins, Cell Line, Chlorocebus aethiops, Dyneins, HeLa Cells, Humans, Luminescent Proteins, Lysosomes, Microscopy, Fluorescence, Models, Biological, Molecular Sequence Data, Mutation, Signal Transduction, Phosphatidylinositol Phosphates, Mice, Knockout, COS Cells, rab GTP-Binding Proteins, Fluorescence Recovery After Photobleaching, Adaptor Proteins, Signal Transducing, Transient Receptor Potential Channels, Apoptosis Regulatory Proteins, HEK293 Cells

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A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation

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