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Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery

Published online by Cambridge University Press:  01 February 1999

BRIAN K. KAY ,
MONTAROP YAMABHAI ,
BEVERLY WENDLAND  and
SCOTT D. EMR
BRIAN K. KAY
Affiliation:
Department of Pharmacology, University of Wisconsin-Madison, Madison, Wisconsin 53706-1532
MONTAROP YAMABHAI
Affiliation:
Department of Pharmacology, University of Wisconsin-Madison, Madison, Wisconsin 53706-1532
BEVERLY WENDLAND
Affiliation:
Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218
SCOTT D. EMR
Affiliation:
Division of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California, San Diego, School of Medicine, La Jolla, California 92093-0668
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Abstract

We have identified a ∼140 amino acid domain that is shared by a variety of proteins in budding and fission yeast, nematode, rat, mouse, frog, oat, and man. Typically, this domain is located within 20 residues of the N-terminus of the various proteins. The percent identity among the domains in the 12 proteins ranges from 42 to 93%, with 16 absolutely conserved residues: N-x11–13-V-x2-A-T-x34–36-R-x7–8-W-R-x3-K-x12-G-x-E-x15-L-x11–12-D-x-G-R-x11-D-x7-R. Even though these proteins share little beyond their segment of homology, data are emerging that several of the proteins are involved in endocytosis and or regulation of cytoskeletal organization. We have named this protein segment the ENTH domain, for Epsin N-terminal Homology domain, and hypothesize that it is a candidate for binding specific ligands and/or enzymatic activity in the cell.

Keywords

Af10clathrincytoskeletonDap160DPFDPWEH domainsendocytosisEps15EpsinhomologyintersectinMP90NPFPan1protein–protein interaction
Type
FOR THE RECORD
Information
Protein Science , Volume 8 , Issue 2 , February 1999 , pp. 435 - 438
Copyright
© 1999 The Protein Society

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