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Originally published In Press as doi:10.1074/jbc.M210504200 on November 25, 2002

J. Biol. Chem., Vol. 278, Issue 7, 4561-4565, February 14, 2003
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Role of the ErbB-4 Carboxyl Terminus in gamma -Secretase Cleavage*

Chang-Yuan NiDagger , Hongping YuanDagger , and Graham CarpenterDagger §

From the Departments of Dagger  Biochemistry and § Medicine, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146

The ErbB-4 receptor tyrosine kinase has a PDZ domain recognition motif at its carboxyl terminus. The first step in ErbB-4 proteolytic processing is a metalloprotease-dependent cleavage of the receptor ectodomain, which is not influenced by deletion of this motif. Metalloprotease cleavage of ErbB-4 produces a membrane-associated 80-kDa fragment that is a substrate for subsequent gamma -secretase cleavage, which releases the cytoplasmic domain from the membrane and allows nuclear translocation of this fragment. Deletion of the PDZ domain recognition motif does abrogate the gamma -secretase cleavage of ErbB-4. The wild-type 80-kDa ErbB-4 fragment forms an association complex with presenilin, thought to be the catalytic moiety of gamma -secretase activity. However, this association is significantly impaired by loss of the PDZ domain recognition motif from ErbB-4. Deletion of this ErbB-4 motif prevents the nuclear localization of the ErbB-4 cytoplasmic domain. Data also show that the basal cleavage of wild-type ErbB-4 by this proteolytic system can produce a sufficient level of ErbB-4 processing to negatively influence cell growth and that loss of the PDZ domain recognition motif abrogates this response.

* This work was supported by National Institutes of Health Grant CA97456. Also, core facility support (Grants CA68485 and DK20593) for the cell imaging shared resource at Vanderbilt University is acknowledged.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.

To whom correspondence should be addressed. Tel.: 615-322-6678; Fax: 615-322-2931; E-mail: graham.carpenter@vanderbilt.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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