| First Author | Yamanashi Y | Year | 1997 |
| Journal | Cell | Volume | 88 |
| Issue | 2 | Pages | 205-11 |
| PubMed ID | 9008161 | Mgi Jnum | J:40721 |
| Mgi Id | MGI:892055 | Doi | 10.1016/s0092-8674(00)81841-3 |
| Citation | Yamanashi Y, et al. (1997) Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok. Cell 88(2):205-11 |
| abstractText | 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. |
