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Publication : Molecular cloning of the CD45-associated 30-kDa protein.

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.
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