Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein.

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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, B-Lymphocytes, Blotting, Western, Bone Marrow Cells, COS Cells, Carrier Proteins, Cell Division, Cell Line, Cell Separation, Cloning, Molecular, DNA, Complementary, Flow Cytometry, Janus Kinase 2, Mice, Models, Genetic, Molecular Sequence Data, Open Reading Frames, Peptides, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, RNA, Messenger, Sequence Homology, Amino Acid, Signal Transduction, T-Lymphocytes, Tissue Distribution, Transfection, Tumor Cells, Cultured, src Homology Domains
Mol. Cell. Biol.
Date: Nov. 01, 2002
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