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Originally published In Press as doi:10.1074/jbc.M110047200 on November 20, 2001

J. Biol. Chem., Vol. 277, Issue 4, 2897-2907, January 25, 2002
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Identification of Developmentally Expressed Proteins That Functionally Interact with Nedd4 Ubiquitin Ligase*

Rodolfo MurillasDagger , Kimberly S. SimmsDagger , Shigetsugu Hatakeyama§, Allan M. Weissman§, and Michael R. KuehnDagger ||

From the Dagger  Experimental Immunology Branch, NCI, National Institutes of Health, Bethesda, Maryland 20892-1360 and the § Regulation of Protein Function Laboratory, NCI, National Institutes of Health, Bethesda, Maryland 20892-1152

Nedd4 is a HECT domain-containing ubiquitin ligase that mediates ubiquitylation and proteasome degradation of target proteins. The molecular basis for the interaction of Nedd4 with substrates lies in its WW domains, which can bind proline-rich (PY) domains in target proteins. Nedd4 is a developmentally expressed protein and may have a fundamental role to play in embryonic processes. However, whether Nedd4 has such a function is currently unknown, in part because few developmentally regulated ubiquitylation substrates have been identified or characterized. We have carried out a yeast two-hybrid screen and identified four proteins expressed in the mid-gestation embryo that are able to interact with Nedd4. Characterization of their functional interaction with Nedd4 in vitro and in vivo demonstrated that three of the four are bona fide Nedd4 binding partners, and two have the capacity to be ubiquitylation substrates. One of these is the first identified nonviral substrate for Nedd4-mediated monoubiquitylation. Interestingly, neither of these two ubiquitylated proteins interacts with Nedd4 through PY-mediated mechanisms. For one of the three Nedd4 binding partners, there was no discernable evidence of ubiquitylation. However, this protein clearly associates with Nedd4 through its PY domains and can alter the location of Nedd4 in cells, suggesting a role other than as a ubiquitylation substrate.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Current address: Dept. of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.

|| To whom correspondence should be addressed: Bldg. 10/Rm. 4B-36, 10 Center Dr., Bethesda, MD 20892-1360. Tel.: 301-435-6476; Fax: 301-496-0887; E-mail: mkuehn@mail.nih.gov.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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