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J. Biol. Chem. Mar (1995); 270(13):7359-64
A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/threonine kinase via an SH3 domain.
Chou MM, Hanafusa H
Laboratory of Molecular Oncology, Rockefeller University, New York, New York 10021, USA.
Abstract: We have previously shown that overexpression of the SH2- and SH3-containing Nck adaptor protein causes transformation of mammalian fibroblast. To elucidate the mechanism by which it deregulates growth, we have sought to identify potential effectors for Nck. We report that a serine/threonine kinase, which we term NAK (for Nck-associated kinase), associates with Nck in vivo and in vitro. Using glutathione S-transferase fusion proteins generated with isolated domains of Nck, we demonstrate that NAK binds specifically to the second of Nck's three SH3 domains. NAK is complexed with Nck in a wide variety of cell types, including NIH3T3, A431, PC12, and Hela cells.
[PUBMED: 7706279] Download Biogrid Interactions in a variety of formats including PSI FormatPUBMED
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.