| First Author | Carpino N | Year | 2002 |
| Journal | Mol Cell Biol | Volume | 22 |
| Issue | 21 | Pages | 7491-500 |
| PubMed ID | 12370296 | Mgi Jnum | J:79606 |
| Mgi Id | MGI:2388544 | Doi | 10.1128/MCB.22.21.7491-7500.2002 |
| Citation | Carpino N, et al. (2002) Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein. Mol Cell Biol 22(21):7491-500 |
| abstractText | In a screen for proteins that interact with Jak2, we identified a previously uncharacterized 70-kDa protein and cloned the corresponding cDNA. The predicated sequence indicates that p70 contains an SH3 domain and a C-terminal domain with similarities to the catalytic motif of phosphoglycerate mutase. p70 transcripts were found in all tissues examined. Similarly, when an antibody raised against a C-terminal peptide to analyze p70 protein expression was used, all murine tissues examined were found to express p70. To investigate the in vivo role of p70, we generated a p70-deficient mouse strain. Mice lacking p70 are viable, develop normally, and do not display any obvious abnormalities. No differences were detected in various hematological parameters, including bone marrow colony-forming ability, in response to cytokines that utilize Jak2. In addition, no impairment in B- and T-cell development and proliferative ability was detected. |
