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J Biol Chem, Vol. 275, Issue 17, 12446-12452, April 28, 2000

Multiple Interactions between Receptor Protein-tyrosine Phosphatase (RPTP) alpha  and Membrane-distal Protein-tyrosine Phosphatase Domains of Various RPTPs*

Christophe Blanchetot and Jeroen den HertogDagger

From the Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands

Receptor protein-tyrosine phosphatase (RPTP) alpha  belongs to the large family of receptor protein-tyrosine phosphatases containing two tandem phosphatase domains. Most of the catalytic activity is retained in the first, membrane-proximal domain (RPTPalpha -D1), and little is known about the function of the second, membrane-distal domain (RPTPalpha -D2). We investigated whether proteins bound to RPTPalpha using the two-hybrid system and found that the second domain of RPTPsigma interacted with the juxtamembrane domain of RPTPalpha . We confirmed this interaction by co-immunoprecipitation experiments. Furthermore, RPTPalpha not only interacted with RPTPsigma -D2 but also with RPTPalpha -D2, LAR-D2, RPTPdelta -D2, and RPTPµ-D2, members of various RPTP subfamilies, although with different affinities. In the yeast two-hybrid system and in glutathione S-transferase pull-down assays, we show that the RPTP-D2s interacted directly with the wedge structure of RPTPalpha -D1 that has been demonstrated to be involved in inactivation of the RPTPalpha -D1/RPTPalpha -D1 homodimer. The interaction was specific because the equivalent wedge structure in LAR was unable to interact with RPTPalpha -D2 or LAR-D2. In vivo, we show that other interaction sites exist as well, including the C terminus of RPTPalpha -D2. The observation that RPTPalpha , but not LAR, bound to multiple RPTP-D2s with varying affinities suggests a specific mechanism of cross-talk between RPTPs that may regulate their biological function.

* 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. Tel.: 31-302121800; Fax: 31-302516464; E-mail: hertog@niob.knaw.nl.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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