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Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
Abstract
During endocytosis, clathrin and the clathrin adaptor protein AP-2, assisted by a variety of accessory factors, help to generate an invaginated bud at the cell membrane. One of these factors is Eps15, a clathrin-coat-associated protein that binds the alpha-adaptin subunit of AP-2. Here we investigate the function of Eps15 by characterizing an important binding partner for its region containing EH domains; this protein, epsin, is closely related to the Xenopus mitotic phosphoprotein MP90 and has a ubiquitous tissue distribution. It is concentrated together with Eps15 in presynaptic nerve terminals, which are sites specialized for the clathrin-mediated endocytosis of synaptic vesicles. The central region of epsin binds AP-2 and its carboxy-terminal region binds Eps15. Epsin is associated with clathrin coats in situ, can be co-precipitated with AP-2 and Eps15 from brain extracts, but does not co-purify with clathrin coat components in a clathrin-coated vesicle fraction. When epsin function is disrupted, clathrin-mediated endocytosis is blocked. We propose that epsin may participate, together with Eps15, in the molecular rearrangement of the clathrin coats that are required for coated-pit invagination and vesicle fission.
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The behavior of GST-Dab2 closely parallels that of GST-epsin 1(1-407) in these assays, showing that Dab2 can function analogously to known endocytic accessory proteins.
“The behavior of GST±Dab2 closely parallels that of a GST±epsin 1(1±407) fusion in these assays (Figure 8C, lanes k±n), showing that Dab2 can function analogously to known endocytic accessory proteins (Chen et al., 1998;Yamabhai et al., 1998;Drake et al., 2000;Mishra et al., 2001).”
From Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor (2002) · cites this paper as Chen et al., 1998
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Metadata
- Authors
- Chen, H., Fre, S., Slepnev, V. I., Capua, M. R., Takei, K., Butler, M. H., Di Fiore, P. P., & De Camilli, P.
- Venue
- Nature
- Published
- 1998-08
- Volume
- 394
- Issue
- 6695
- Pages
- 793-797
- ISSN
- 0028-0836
- 1476-4687
- Cited by
- 425
- References
- 0
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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