Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis

Hong Chen, Silvia Fre, Vladimir I. Slepnev, Maria Rosaria Capua, Kohji Takei, Margaret H. Butler, Pier Paolo Di Fiore, Pietro De Camilli

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Abstract

During endocytosis, clathrin and the clathrin adaptor protein AP-2 (ref.1), 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 α-adaptin subunit of AP-2 (refs 4-8). 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 (ref. 10) 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.

Original languageEnglish
Pages (from-to)793-797
Number of pages5
JournalNature
Volume394
Issue number6695
DOIs
Publication statusPublished - Aug 20 1998
Externally publishedYes

ASJC Scopus subject areas

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    Chen, H., Fre, S., Slepnev, V. I., Capua, M. R., Takei, K., Butler, M. H., Di Fiore, P. P., & De Camilli, P. (1998). Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature, 394(6695), 793-797. https://doi.org/10.1038/29555