Abstract
Endocytosis is a process through which extracellular materials are transported into cell through membrane deformation. This process is not a simple step-by-step process in which a series of proteins function according to the chronological order, but rather a complex process comprising many members which are regulated precisely. The role of endocytosis is broadly divided into two categories, phagocytosis and pinocytosis, the latter is divided into four species in accordance with the size of endocytosis substances: clathrin dependent endocytosis, the diameter of clathrin-coated vesicle is 100–150 nm; caveolin dependent endocytosis, the diameter of caveolin protein-coated vesicle is 50–100 nm; macropinocytosis, the diameter of macropinocytosis is generally 0.5–2 μm, sometimes up to 5 μm; clathrin and caveolin independent endocytosis. Many proteins including endophilin A1, A2, A3, and endocytotic proteins B, B1a, and B1b as well as dynamin, actin and Rab protein families are involved in endocytosis and play an important role in different stages. The abnormal endocytosis may be involved in the development of certain diseases.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
Giodini A, Rahner C, Cresswell P. Receptor-mediated phagocytosis elicits cross-presentation in nonprofessional antigen-presenting cells. Proc Natl Acad Sci USA, 2009, 106: 3324–3329.
Kirchhausen T. Clathrin. Annu Rev Biochem, 2000, 69: 699–727.
Kiss AL, Turi A, Müller N, et al. Caveolae and caveolin isoforms in rat peritoneal macrophages. Micron, 2002, 33: 75–93.
Rajjayabun PH, Garg S, Durkan GC, et al. Caveolin-1 expression is associated with high-grade bladder cancer. Urology, 2001, 58: 811–814.
Frank PG, Woodman SE, Park DS, et al. Caveolin, caveolae and endothelial cell function. Arterioscler Thromb Vasc Biol, 2003, 23: 1161–1168.
Krajewska WM, Masłowska I. Caveolins: structure and function in signal transduction. Cell Mol Biol Lett, 2004, 9: 195–220.
Pascariu M, Bendayan M, Ghitescu L. Correlated endothelial caveolin overexpression and increased transcytosis in experimental diabetes. J Histochem Cytochem, 2004, 52: 65–76.
Fra AM, Pasqualetto E, Mancini M, et al. Genomic organization and transcriptional analysis of the human genes coding for caveolin-1 and caveolin-2. Gene, 2000, 243: 75–83.
Cameron PL, Liu C, Smart DK, et al. Caveolin-1 expression is maintained in rat and human astroglioma cell lines. Glia, 2002, 37: 275–290.
Williams TM, Cheung MW, Park DS, et al. Loss of caveolin-1 gene expression accelerates the development of dysplastic mammary lesions in tumor-prone transgenic mice. Mol Biol Cell, 2003, 14: 1027–1042.
Gaudreault SB, Dea D, Poirier J. Increased caveolin-1 expression in Alzheimer’s disease brain. Neurobiol Aging, 2004, 25: 753–759.
Müller JS, Piko H, Schoser BG, et al. Novel splice site mutation in the caveolin-3 gene leading to autosomal recessive limb girdle muscular dystrophy. Neuromuscul Disord, 2006, 16: 432–436.
Lim JP, Wang JT, Kerr MC, et al. A role for SNX5 in the regulation of macropinocytosis. BMC Cell Biol, 2008, 9: 58.
Miki H, Yamaguchi H, Suetsugu S, et al. IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature, 2000, 408: 732–735.
Sun P, Yamamoto H, Suetsugu S, et al. Small GTPase Rah/Rab34 is associated with membrane ruffles and macropinosomes and promotes macropinosome formation. J Biol Chem, 2003, 278: 4063–4071.
Daniels RL, Takashima Y, McKemy DD. Activity of the neuronal cold sensor TRPM8 is regulated by phospholipase C via the phospholipid phosphoinositol 4,5-bisphosphate. J Biol Chem, 2009, 284: 1570–1582.
Gad H, Ringstad N, Löw P, et al. Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin. Neuron, 2000, 27: 301–312.
Petrelli A, Gilestro GF, Lanzardo S, et al. The endophilin-CIN85-Cb1 complex mediates ligand-dependent downregulation of c-Met. Nature, 2002, 416: 187–190.
Williams R. PIP2 in endocytosis. J Cell Biol, 2007, 177: 185.
Guichet A, Wucherpfennig T, Dudu V, et al. Essential role of endophilin A in synaptic vesicle budding at the Drosophila neuromuscular junction. EMBO J, 2002, 21: 1661–1672.
Takei K, McPherson PS, Schmid SL, et al. Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature, 1995, 374: 186–190.
Zhang X, Wang F, Chen X, et al. Post-endocytic fates of delta-opioid receptor are regulated by GRK2-mediated receptor phosphorylation and distinct beta-arrestin isoforms. J Neurochem, 2008, 106: 781–792.
William A. Twisting endocytosis. J Cell Biol, 2006, 173: 456.
Damke H, Binns DD, Ueda H, et al. Dynamin GTPase domain mutants block endocytic vesicle formation at morphologically distinct stages. Mol Biol Cell, 2001, 12: 2578–2589.
Tsujita K, Suetsugu S, Sasaki N, et al. Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J Cell Biol, 2006, 172: 269–279.
Sun Y, Martin AC, Drubin DG. Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity. Dev Cell, 2006, 11: 33–46.
Okreglak V, Drubin DG. Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state. J Cell Biol, 2007, 178: 1251–1264.
Kaksonen M, Toret CP, Drubin DG. A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell, 2005, 123: 305–320.
O’Keeffe MB, Reid HM, Kinsella BT. Agonist-dependent internalization and trafficking of the human prostacyclin receptor: a direct role for Rab5a GTPase. Biochim Biophys Acta, 2008, 1783: 1914–1928.
Author information
Authors and Affiliations
Corresponding author
Additional information
Supported by grants from the National Natural Sciences Foundation of China (No. 30771126 and 30772106).
Rights and permissions
About this article
Cite this article
Chen, L., Li, H., Zhao, R. et al. Study progress of cell endocytosis. Chin. -Ger. J. Clin. Oncol. 8, 360–365 (2009). https://doi.org/10.1007/s10330-009-0023-9
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10330-009-0023-9