Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok.
A 62 kDa protein is highly phosphorylated in many cells containing activated tyrosine kinases. This protein, characterized mainly by its avid association with rasGAP, has proved elusive. Anti-phosphotyrosine antibody was used to purify p62. From peptide sequence, molecular cloning revealed a cDNA encoding a novel protein, p62dok, with little homology ... to others but with a prominent set of tyrosines and nearby sequences suggestive of SH2 binding sites. In cells, v-Abl tyrosine kinase binds and strongly phosphorylates p62dok, which then binds rasGAP. A monoclonal antibody, 2C4, to the rasGAP-associated p62 reacts with p62dok. Thus, p62dok appears to be the long-sought major substrate of many tyrosine kinases.
Mesh Terms:
Amino Acid Sequence, Animals, Antibodies, Monoclonal, Binding Sites, Blotting, Northern, Cell Line, Cell Line, Transformed, Cloning, Molecular, DNA, Complementary, DNA-Binding Proteins, GTPase-Activating Proteins, Mice, Molecular Sequence Data, Oncogene Proteins v-abl, Phosphoproteins, Phosphorylation, Phosphotyrosine, Protein-Tyrosine Kinases, Proteins, RNA-Binding Proteins, Sequence Homology, Amino Acid, Transfection, src Homology Domains
Amino Acid Sequence, Animals, Antibodies, Monoclonal, Binding Sites, Blotting, Northern, Cell Line, Cell Line, Transformed, Cloning, Molecular, DNA, Complementary, DNA-Binding Proteins, GTPase-Activating Proteins, Mice, Molecular Sequence Data, Oncogene Proteins v-abl, Phosphoproteins, Phosphorylation, Phosphotyrosine, Protein-Tyrosine Kinases, Proteins, RNA-Binding Proteins, Sequence Homology, Amino Acid, Transfection, src Homology Domains
Cell
Date: Jan. 24, 1997
PubMed ID: 9008161
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