First Author | Takeda A | Year | 1994 |
Journal | J Biol Chem | Volume | 269 |
Issue | 4 | Pages | 2357-60 |
PubMed ID | 8300558 | Mgi Jnum | J:16674 |
Mgi Id | MGI:64741 | Doi | 10.1016/s0021-9258(17)41950-8 |
Citation | Takeda A, et al. (1994) Molecular cloning of the CD45-associated 30-kDa protein. J Biol Chem 269(4):2357-60 |
abstractText | CD45, a leukocyte-specific transmembrane protein tyrosine phosphatase, mediates signal transduction pathways critical for immune responses. However, the mechanism of CD45-mediated signal transduction and the identity of CD45-associated proteins have remained unclear. A CD45-associated 30-kDA phosphorylated protein (CD45-AP) was purified by virtue of its specific association with CD45, and its mouse cDNA was cloned by using the internal amino acid sequence information. In vitro translated CD45-AP bound specifically to CD45. CD45-AP appears to be leukocyte-specific and shares no significant homology with presently known sequences. The predicted sequence contains no consensus tyrosine phosphorylation sites or conserved sequences of GTP-binding proteins. CD45-AP may act as an adapter molecule for CD45-mediated signal transduction. |