Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis.
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.
Mesh Terms:
Adaptor Protein Complex alpha Subunits, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Animals, Blotting, Northern, Brain, CHO Cells, Calcium-Binding Proteins, Carrier Proteins, Clathrin, Cricetinae, Endocytosis, Membrane Proteins, Molecular Sequence Data, Neuropeptides, Phosphoproteins, Protein Binding, Rats, Recombinant Fusion Proteins, Transfection, Vesicular Transport Proteins
Adaptor Protein Complex alpha Subunits, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Animals, Blotting, Northern, Brain, CHO Cells, Calcium-Binding Proteins, Carrier Proteins, Clathrin, Cricetinae, Endocytosis, Membrane Proteins, Molecular Sequence Data, Neuropeptides, Phosphoproteins, Protein Binding, Rats, Recombinant Fusion Proteins, Transfection, Vesicular Transport Proteins
Nature
Date: Aug. 20, 1998
PubMed ID: 9723620
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