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.
Mesh Terms:
3T3 Cells, Adaptor Proteins, Signal Transducing, Amino Acids, Animals, Binding Sites, Cell Division, Cell Line, Transformed, Cell Membrane, Electrophoresis, Polyacrylamide Gel, Genes, src, Glutathione Transferase, Hela Cells, Humans, Ligands, Mice, Oncogene Proteins, Oncogenes, PC12 Cells, Phosphoproteins, Protein-Serine-Threonine Kinases, Rats, Recombinant Fusion Proteins, Substrate Specificity
3T3 Cells, Adaptor Proteins, Signal Transducing, Amino Acids, Animals, Binding Sites, Cell Division, Cell Line, Transformed, Cell Membrane, Electrophoresis, Polyacrylamide Gel, Genes, src, Glutathione Transferase, Hela Cells, Humans, Ligands, Mice, Oncogene Proteins, Oncogenes, PC12 Cells, Phosphoproteins, Protein-Serine-Threonine Kinases, Rats, Recombinant Fusion Proteins, Substrate Specificity
J. Biol. Chem.
Date: Mar. 31, 1995
PubMed ID: 7706279
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