Carpino, N., Kobayashi, R., Zang, H., Takahashi, Y., Jou, S. T., Feng, J., Nakajima, H., Ihle, J. N. (November 2002) Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein. Molecular and Cellular Biology, 22 (21). pp. 7491-7500. ISSN 0270-7306
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Abstract
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.
Item Type: | Paper |
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Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification Investigative techniques and equipment > cloning Investigative techniques and equipment > assays > cloning bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > SH3 domain |
CSHL Authors: | |
Communities: | CSHL labs > Kobayashi lab |
Depositing User: | Matt Covey |
Date: | November 2002 |
Date Deposited: | 09 Jan 2014 14:37 |
Last Modified: | 09 Jan 2014 14:37 |
PMCID: | PMC135669 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/28682 |
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