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 and Pietro De Camilli ()
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Hong Chen: Yale University School of Medicine
Silvia Fre: European Institute of Oncology
Vladimir I. Slepnev: Yale University School of Medicine
Maria Rosaria Capua: European Institute of Oncology
Kohji Takei: Yale University School of Medicine
Margaret H. Butler: Yale University School of Medicine
Pier Paolo Di Fiore: European Institute of Oncology
Pietro De Camilli: Yale University School of Medicine

Nature, 1998, vol. 394, issue 6695, 793-797

Abstract: 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 membrane2,3. One of these factors is Eps15, a clathrin-coat-associated protein that binds the α-adaptin subunit of AP-2 (4–8). Here we investigate the function of Eps15 by characterizing an important binding partner for its region containing EH domains9; 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.

Date: 1998
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DOI: 10.1038/29555

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