TY - JOUR
T1 - Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
AU - Chen, Hong
AU - Fre, Silvia
AU - Slepnev, Vladimir I.
AU - Capua, Maria Rosaria
AU - Takei, Kohji
AU - Butler, Margaret H.
AU - Di Fiore, Pier Paolo
AU - De Camilli, Pietro
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1998/8/20
Y1 - 1998/8/20
N2 - 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.
AB - 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.
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U2 - 10.1038/29555
DO - 10.1038/29555
M3 - Article
C2 - 9723620
AN - SCOPUS:0032552056
VL - 394
SP - 793
EP - 797
JO - Nature
JF - Nature
SN - 0028-0836
IS - 6695
ER -