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Role of Phospholipids in Endocytosis, Phagocytosis, and Macropinocytosis
Abstract
Endocytosis, phagocytosis, and macropinocytosis are fundamental processes that enable cells to sample their environment, eliminate pathogens and apoptotic bodies, and regulate the expression of surface components. While a great deal of effort has been devoted over many years to understanding the proteins involved in these processes, the important contribution of phospholipids has only recently been appreciated. This review is an attempt to collate and analyze the rapidly emerging evidence documenting the role of phospholipids in clathrin-mediated endocytosis, phagocytosis, and macropinocytosis. A primer on phospholipid biosynthesis, catabolism, subcellular distribution, and transport is presented initially, for reference, together with general considerations of the effects of phospholipids on membrane curvature and charge. This is followed by a detailed analysis of the critical functions of phospholipids in the internalization processes and in the maturation of the resulting vesicles and vacuoles as they progress along the endo-lysosomal pathway.
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Cites
Gut flora metabolism of phosphatidylcholine promotes cardiovascular disease
Wang, Z., Klipfell, E., Bennett, B. J., Koeth, R., Levison, B. S., DuGar, B., Feldstein, A. E., Britt, E. B., Fu, X., Chung, Y.-M., et al. (2011) · Nature · doi:10.1038/nature09922 · Cited by 5,597
Autophagy regulates lipid metabolism
Singh, R., Kaushik, S., Wang, Y., Xiang, Y., Novak, I., Komatsu, M., Tanaka, K., Cuervo, A. M., & Czaja, M. J. (2009) · Nature · doi:10.1038/nature07976 · Cited by 3,975
Autophagy in immunity and inflammation
Levine, B., Mizushima, N., & Virgin, H. W. (2011) · Nature · doi:10.1038/nature09782 · Cited by 3,289
Doherty, G. J., & McMahon, H. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081307.110540 · Cited by 3,075
Phosphoinositides in cell regulation and membrane dynamics
Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790
Targeting PI3K signalling in cancer: opportunities, challenges and limitations
Engelman, J. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2664 · Cited by 2,445
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
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
Tanida, I., Ueno, T., & Kominami, E. (2008) · Methods in Molecular Biology™ · doi:10.1007/978-1-59745-157-4_4 · Cited by 1,785
The emerging mechanisms of isoform-specific PI3K signalling
Vanhaesebroeck, B., Guillermet-Guibert, J., Graupera, M., & Bilanges, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2882 · Cited by 1,767
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275
Identification of Tim4 as a phosphatidylserine receptor
Miyanishi, M., Tada, K., Koike, M., Uchiyama, Y., Kitamura, T., & Nagata, S. (2007) · Nature · doi:10.1038/nature06307 · Cited by 1,180
Phosphatidic Acid-Mediated Mitogenic Activation of mTOR Signaling
Fang, Y., Vilella-Bach, M., Bachmann, R., Flanigan, A., & Chen, J. (2001) · Science · doi:10.1126/science.1066015 · Cited by 1,055
Regulation of Phagosome Maturation by Signals from Toll-Like Receptors
Blander, J. M., & Medzhitov, R. (2004) · Science · doi:10.1126/science.1096158 · Cited by 991
Protein kinase C and other diacylglycerol effectors in cancer
Griner, E. M., & Kazanietz, M. G. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2110 · Cited by 978
Araki, N., Johnson, M. T., & Swanson, J. A. (1996) · The Journal of cell biology · doi:10.1083/jcb.135.5.1249 · Cited by 949 · cited 3×
“Like CME, macropinocytosis generates fluid-filled vacuoles but, similar to phagocytosis, it requires large-scale actin remodeling and PtdInsP3K activity (17).”
BackgroundInfluentialShaping cups into phagosomes and macropinosomes
Swanson, J. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2447 · Cited by 941
Plasma membrane contributes to the formation of pre-autophagosomal structures
Ravikumar, B., Moreau, K., Jahreiss, L., Puri, C., & Rubinsztein, D. C. (2010) · Nature Cell Biology · doi:10.1038/ncb2078 · Cited by 902
Plasma membrane phosphoinositide organization by protein electrostatics
McLaughlin, S., & Murray, D. (2005) · Nature · doi:10.1038/nature04398 · Cited by 868
The Rab5 effector EEA1 is a core component of endosome docking
Christoforidis, S., McBride, H. M., Burgoyne, R. D., & Zerial, M. (1999) · Nature · doi:10.1038/17618 · Cited by 854
PIP2and Proteins: Interactions, Organization, and Information Flow
McLaughlin, S., Wang, J., Gambhir, A., & Murray, D. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.082901.134259 · Cited by 837
p53 and Pten control neural and glioma stem/progenitor cell renewal and differentiation
Zheng, H., Ying, H., Yan, H., Kimmelman, A. C., Hiller, D. J., Chen, A.-J., Perry, S. R., Tonon, G., Chu, G. C., Ding, Z., et al. (2008) · Nature · doi:10.1038/nature07443 · Cited by 767
A High Precision Survey of the Molecular Dynamics of Mammalian Clathrin-Mediated Endocytosis
Taylor, M. J., Perrais, D., & Merrifield, C. J. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000604 · Cited by 754
A Modular Design for the Clathrin- and Actin-Mediated Endocytosis Machinery
Kaksonen, M., Toret, C. P., & Drubin, D. G. (2005) · Cell · doi:10.1016/j.cell.2005.09.024 · Cited by 726
Role of LBPA and Alix in Multivesicular Liposome Formation and Endosome Organization
Matsuo, H., Chevallier, J., Mayran, N., Le Blanc, I., Ferguson, C., Fauré, J., Blanc, N. S., Matile, S., Dubochet, J., Sadoul, R., et al. (2004) · Science · doi:10.1126/science.1092425 · Cited by 705
Fab1p PtdIns(3)P 5-Kinase Function Essential for Protein Sorting in the Multivesicular Body
Odorizzi, G., Babst, M., & Emr, S. D. (1998) · Cell · doi:10.1016/s0092-8674(00)81707-9 · Cited by 656
Gaullier, J.-M., Simonsen, A., D'Arrigo, A., Bremnes, B., Stenmark, H., & Aasland, R. (1998) · Nature · doi:10.1038/28767 · Cited by 553
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
Self-citationMcBride, H. M., Rybin, V., Murphy, C., Giner, A., Teasdale, R., & Zerial, M. (1999) · Cell · doi:10.1016/s0092-8674(00)81966-2 · Cited by 520
Life — As a Matter of Fat: The Emerging Science of Lipidomics
Mouritsen, O. G. (2005) · The Frontiers Collection · doi:10.1007/b138577 · Cited by 448
Stamnes, M. A., & Rothman, J. E. (1993) · Cell · doi:10.1016/0092-8674(93)90277-w · Cited by 416
Kiefer, F., Brumell, J., Al-Alawi, N., Latour, S., Cheng, A., Veillette, A., Grinstein, S., & Pawson, T. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.4209 · Cited by 376
Self-citationListeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles
Birmingham, C. L., Canadien, V., Kaniuk, N. A., Steinberg, B. E., Higgins, D. E., & Brumell, J. H. (2008) · Nature · doi:10.1038/nature06479 · Cited by 330
Receptor Activation Alters Inner Surface Potential During Phagocytosis
Yeung, T., Terebiznik, M., Yu, L., Silvius, J., Abidi, W. M., Philips, M., Levine, T., Kapus, A., & Grinstein, S. (2006) · Science · doi:10.1126/science.1129551 · Cited by 329
Self-citationThe Mechanochemistry of Endocytosis
Liu, J., Sun, Y., Drubin, D. G., & Oster, G. F. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000204 · Cited by 222
Ghazizadeh, S., Bolen, J. B., & Fleit, H. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37050-3 · Cited by 202
Genetic disorders of adipose tissue development, differentiation, and death.
Agarwal, A. K., & Garg, A. (2006) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.7.080505.115715 · Cited by 150
Phospholipase C–mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane
Hao, J.-J., Liu, Y., Kruhlak, M., Debell, K. E., Rellahan, B. L., & Shaw, S. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200807047 · Cited by 137
Kusner, D. J., Hall, C. F., & Jackson, S. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.4.2266 · Cited by 75
Horan, K. A., Watanabe, K.-I., Kong, A. M., Bailey, C. G., Rasko, J. E. J., Sasaki, T., & Mitchell, C. A. (2007) · Blood · doi:10.1182/blood-2007-02-073874 · Cited by 45
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Clathrin-independent pathways of endocytosis
Mayor, S., Parton, R. G., & Donaldson, J. G. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016758 · Cited by 525
PI3K signalling in inflammation
Hawkins, P. T., & Stephens, L. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.12.006 · Cited by 541
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Caicedo, A., Aponte, P. M., Cabrera, F., Hidalgo, C., & Khoury, M. (2017) · Stem Cells International · doi:10.1155/2017/7610414 · Cited by 150
Metadata
- Authors
- Bohdanowicz, M., & Grinstein, S.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2013-01
- Volume
- 93
- Issue
- 1
- Pages
- 69-106
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2096727743
- Cited by
- 311
- References
- 40
- FWCI
- 3.15
- Type
- journal article
- Language
- en
- Open access
- closed
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