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Cited by 72

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Epsin: Inducing membrane curvature

Horvath, Caroline A.J., Vanden Broeck, Davy, Boulet, Gaëlle A.V., Bogers, Johannes, De Wolf, Marc J.S.·2007·The International Journal of Biochemistry & Cell Biology
DOI 10.1016/j.biocel.2006.12.004
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Abstract

Epsin was originally discovered by virtue of its binding to another accessory protein, Eps15. Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. Epsin isoforms have been described that differ in intracellular site of action and/or in tissue distribution, although all epsins essentially contribute to membrane deformation. Besides inducing membrane curvature, epsin also plays a key function as adaptor protein, coupling various components of the clathrin-assisted uptake and fulfils an important role in selecting and recognizing cargo. Furthermore, epsin possesses the ability to block vesicle formation during mitosis. To perform all these functions, epsin, apart from interacting with PtdIns(4,5)P2 via its ENTH domain, also engages in several protein interactions with different components of the clathrin-mediated endocytic system. Recently, RNA interference has successfully been exploited to generate a cell line constitutively silencing epsin expression, which can be used to study internalization of multiple ligands.

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Research works printed but not linked: 20

  1. Aguilar, 2006, Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins, Proc. Natl. Acad. Sci., 11, 4116, 10.1073/pnas.0510513103 · DOI
  2. Barriere, 2006, Molecular basis of oligoubiquitin-dependent internalization of membrane proteins in mammalian cells, Traffic, 7, 282, 10.1111/j.1600-0854.2006.00384.x · DOI
  3. Chen, 1998, Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis, Nature, 394, 793, 10.1038/29555 · DOI · Paper page
  4. De Camilli, 2002, The ENTH domain, FEBS Lett., 513, 11, 10.1016/S0014-5793(01)03306-3 · DOI
  5. Hawryluk, 2006, Epsin 1 is a polyubiquitin-selective clathrin-associated sorting protein, Traffic, 7, 262, 10.1111/j.1600-0854.2006.00383.x · DOI
  6. Hurley, 2002, Driving membranes around the bend, Cell, 111, 143, 10.1016/S0092-8674(02)01044-9 · DOI
  7. Hyman, 2000, Epsin 1 undergoes nucleocytosolic shuttling and its Eps15 interactor NH2-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukaemia Zn2+-finger protein (PLFZ), J. Cell Biol., 149, 537, 10.1083/jcb.149.3.537 · DOI · Paper page
  8. Kalthoff, 2002, Clint: A novel clathrin-binding ENTH-domain protein at the Golgi, Mol. Biol. Cell, 13, 4073, 10.1091/mbc.e02-03-0171 · DOI
  9. Kweon, 2006, Membrane topology of helix 0 of the Epsin N-terminal homology domain, Mol. Cells, 30, 428, 10.1016/S1016-8478(23)12873-1 · DOI
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  15. Rosenthal, 1999, The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module, J. Biol. Chem., 274, 33959, 10.1074/jbc.274.48.33959 · DOI
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  17. Spradling, 2001, Epsin 3 is a novel extracellular matrix-induced transcript specific to wounded epithelia, J. Biol. Chem., 276, 29257, 10.1074/jbc.M101663200 · DOI
  18. Vanden Broeck, 2006, Selective blocking of clathrin-mediated endocytosis by RNA interference: Epsin as a target protein, Biotechniques, 41, 475, 10.2144/000112265 · DOI
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Metadata

Authors
Horvath, C. A. J., Vanden Broeck, D., Boulet, G. A. V., Bogers, J., & De Wolf, M. J. S.
Venue
The International Journal of Biochemistry & Cell Biology
Publisher
Elsevier BV
Published
2007
Volume
39
Issue
10
Pages
1765-1770
ISSN
1357-2725
DOI
10.1016/j.biocel.2006.12.004
Cited by
72
References
2
Language
en
Licence

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