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© The Rockefeller University Press, 0021-9525/1998//287 $5.00
The Journal of Cell Biology, Volume 141, Number 1, , 1998 287-296

Dynamic Interaction of PTPµ with Multiple Cadherins In Vivo

Susann M. Brady-Kalnay^*, Tracy Mourton^*, Joseph P. Nixon^*, Gregory E. Pietz^*, Michael Kinch, Haiyan Chen, Robert Brackenbury, David L. Rimm^||, Robert L. Del Vecchio^¶, and Nicholas K. Tonks^¶

^* Department of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, Ohio 44106-4960; Department of Basic Medical Sciences, Purdue University, West Lafayette, Indiana 47097; Department of Cell Biology, Neurobiology and Anatomy, University of Cincinnati, Cincinnati, Ohio 45267; ^|| Department of Pathology, Yale University, New Haven, Connecticut 06510-8023; and ^¶ Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724-2208

There is a growing body of evidence to implicate reversible tyrosine phosphorylation as an important mechanism in the control of the adhesive function of cadherins. We previously demonstrated that the receptor protein tyrosine phosphatase PTPµ associates with the cadherin–catenin complex in various tissues and cells and, therefore, may be a component of such a regulatory mechanism (Brady-Kalnay, S.M., D.L. Rimm, and N.K. Tonks. 1995. J. Cell Biol. 130:977– 986). In this study, we present further characterization of this interaction using a variety of systems. We observed that PTPµ interacted with N-cadherin, E-cadherin, and cadherin-4 (also called R-cadherin) in extracts of rat lung. We observed a direct interaction between PTPµ and E-cadherin after coexpression in Sf9 cells. In WC5 cells, which express a temperature-sensitive mutant form of v-Src, the complex between PTPµ and E-cadherin was dynamic, and conditions that resulted in tyrosine phosphorylation of E-cadherin were associated with dissociation of PTPµ from the complex. Furthermore, we have demonstrated that the COOH-terminal 38 residues of the cytoplasmic segment of E-cadherin was required for association with PTPµ in WC5 cells. Zondag et al. (Zondag, G., W. Moolenaar, and M. Gebbink. 1996. J. Cell Biol. 134: 1513–1517) have asserted that the association we observed between PTPµ and the cadherin–catenin complex in immunoprecipitates of the phosphatase arises from nonspecific cross-reactivity between BK2, our antibody to PTPµ, and cadherins. In this study we have confirmed our initial observation and demonstrated the presence of cadherin in immunoprecipitates of PTPµ obtained with three antibodies that recognize distinct epitopes in the phosphatase. In addition, we have demonstrated directly that the anti-PTPµ antibody BK2 that we used initially did not cross-react with cadherin. Our data reinforce the observation of an interaction between PTPµ and E-cadherin in vitro and in vivo, further emphasizing the potential importance of reversible tyrosine phosphorylation in regulating cadherin function.

Abbreviations used in this paper: GST, glutathione S transferase; PTK, protein tyrosine kinase; PTP, protein tyrosine phosphatase.

Address all correspondence to N.K. Tonks, Cold Spring Harbor Laboratory, One Bungtown Road, Cold Spring Harbor, NY 11724-2208. Tel.: (516) 367-8846. Fax: (516) 367-6812. E-mail: tonks{at}cshl.org

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