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J Biol Chem, Vol. 274, Issue 48, 33959-33965, November 26, 1999
From the Epsin (epsin 1) is an interacting partner for the
EH domain-containing region of Eps15 and has been implicated in
conjunction with Eps15 in clathrin-mediated endocytosis. We report here
the characterization of a similar protein (epsin 2), which we have cloned from human and rat brain libraries. Epsin 1 and 2 are most similar in their NH2-terminal region, which
represents a module (epsin NH2
terminal homology domain, ENTH domain) found in
a variety of other proteins of the data base. The multiple DPW motifs,
typical of the central region of epsin 1, are only partially conserved in epsin 2. Both proteins, however, interact through this central region with the clathrin adaptor AP-2. In addition, we show here that
both epsin 1 and 2 interact with clathrin. The three NPF motifs of the
COOH-terminal region of epsin 1 are conserved in the corresponding
region of epsin 2, consistent with the binding of both proteins to
Eps15. Epsin 2, like epsin 1, is enriched in brain, is present in a
brain-derived clathrin-coated vesicle fraction, is concentrated in the
peri-Golgi region and at the cell periphery of transfected cells, and
partially colocalizes with clathrin. High overexpression of green
fluorescent protein-epsin 2 mislocalizes components of the clathrin
coat and inhibits clathrin-mediated endocytosis. The epsins define a
new protein family implicated in membrane dynamics at the cell surface.
The Epsins Define a Family of Proteins That Interact with
Components of the Clathrin Coat and Contain a New Protein Module
,,,,
Howard Hughes Medical Institute and
Department of Cell Biology, Yale University School of Medicine, New
Haven, Connecticut 06510, § Department of Experimental
Oncology, European Institute of Oncology, Milan 20141, Italy, and
¶ Instituto di Microbiologia Universita' di Bari,
Bari 70124, Italy
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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