A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/threonine kinase via an SH3 domain.
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.
Chou
M M
MM
Laboratory of Molecular Oncology, Rockefeller University, New York, New York 10021, USA.
Hanafusa
H
H
D016475:3T3 Cells; D048868:Adaptor Proteins, Signal Transducing; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002455:Cell Division; D002461:Cell Line, Transformed; D002462:Cell Membrane / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D016391:Genes, src; D005982:Glutathione Transferase / Q000096:biosynthesis / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D008024:Ligands; D051379:Mice; D015513:Oncogene Proteins / Q000096:biosynthesis / Q000378:metabolism*; D009857:Oncogenes; D016716:PC12 Cells; D010750:Phosphoproteins / Q000302:isolation & purification / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000378:metabolism; D013379:Substrate Specificity
D048868:Adaptor Proteins, Signal Transducing; D000596:Amino Acids; D008024:Ligands; C078332:Nck protein; D015513:Oncogene Proteins; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase; D017346:Protein Serine-Threonine Kinases