| First Author | Di Cristofano A | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 9 | Pages | 4827-30 |
| PubMed ID | 9478921 | Mgi Jnum | J:46266 |
| Mgi Id | MGI:1197431 | Doi | 10.1074/jbc.273.9.4827 |
| Citation | Di Cristofano A, et al. (1998) Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins. J Biol Chem 273(9):4827-30 |
| abstractText | Chronic myelogenous leukemia (CML) is a disease characterized by the presence of p210(bcr-abl), a chimeric protein with tyrosine kinase activity. Substrates for p210(bcr-abl) are likely to be involved in the pathogenesis of CML. Here we describe the purification, cDNA cloning, and characterization of a 56-kDa tyrosine phosphorylated protein, p56 (dok-2) (Dok-2), from p210(bcr-abl) expressing cells. The human dok-2 cDNA encodes a 412-amino acid protein with a predicted N-terminal pleckstrin homology domain as well as several other features of a signaling molecule, including 13 potential tyrosine phosphorylation sites, six PXXP motifs, and the ability to bind to p120(RasGAP). Dok-2 was shown to be 35% identical to p62(dok-1), a recently identified RasGAP binding protein from CML cells, and analysis of the expressed sequence tag data base revealed the presence of at least four additional proteins containing a Dok homology sequence motif. Dok mRNAs were primarily expressed in tissues of hematopoietic origin. These findings strongly suggest that a family of Dok-related proteins exists that bind to RasGAP and may mediate the effects of p210(bcr-abl) in CML. |
