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Originally published In Press as doi:10.1074/jbc.M105785200 on July 30, 2001

J. Biol. Chem., Vol. 276, Issue 39, 36535-36542, September 28, 2001
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PDZ Interaction Sites in Integrin alpha  Subunits
TIP-2/GIPC BINDS TO A TYPE I RECOGNITION SEQUENCE IN alpha 6A/alpha 5 AND A NOVEL SEQUENCE IN alpha 6B*

Taneli T. Tani and Arthur M. MercurioDagger

From the Division of Cancer Biology and Angiogenesis, Department of Pathology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215

We used published peptide library data to identify PDZ recognition sequences in integrin alpha  subunit cytoplasmic domains and found that the alpha 6A and alpha 5 subunits contain a type I PDZ binding site (TSDA*) (asterisk indicates the stop codon). The alpha 6A cytoplasmic domain was used for screening a two-hybrid library to find interacting proteins. The bulk of the captured cDNAs (60%) coded for TIP-2/GIPC, a cytoplasmic protein with one PDZ domain. The interaction of TIP-2/GIPC with different integrin subunits was tested in two-hybrid and in vitro binding assays. Surprisingly, TIP-2/GIPC bound strongly to the C terminus of both alpha 6A and alpha 6B, although the alpha 6B sequence (ESYS*) is not suggestive of a PDZ binding site because of its polar C-terminal residue. For high affinity interaction with TIP-2/GIPC, at least one of the residues at positions -1 and -3 must be negatively charged. An aliphatic residue at position 0 increases the affinity of but is not required for this interaction. The alpha 5 integrin subunit also bound to TIP-2/GIPC. The alpha 6 integrin and TIP-2/GIPC co-localize in retraction fibers in carcinoma cells plated on laminin, a finding suggesting a functional interaction in vivo. Our results demonstrate that both splice variants of alpha 6 integrin contain a conserved PDZ binding site that enables interaction with TIP-2/GIPC. The binding site in alpha 6B defines a new subclass of type I PDZ interaction site, characterized by a non-aliphatic residue at position 0.

* This work was supported by United States Army Medical Research and Materiel Command Grant DAMD17-00-1-0155, the Academy of Finland, and the Finnish Cultural Foundation (to T. T. T.) and by National Institutes of Health Grants AI39264 and CA80789 (to A. M. M.).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.

Dagger To whom correspondence should be addressed: Division of Cancer Biology and Angiogenesis, Dept. of Pathology, Beth Israel Deaconess Medical Center and Harvard Medical School, 330 Brookline Ave., Boston, MA 02215. Tel.: 617-667-7714; Fax: 617-975-5531; E-mail: amercuri@caregroup.harvard.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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