Identification, cDNA Cloning, and Targeted Deletion of p70, a Novel, Ubiquitously Expressed SH3 Domain-Containing Protein
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Published:2002-11
Issue:21
Volume:22
Page:7491-7500
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ISSN:0270-7306
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Container-title:Molecular and Cellular Biology
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language:en
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Short-container-title:Mol Cell Biol
Author:
Carpino Nick1, Kobayashi Ryuji2, Zang Heesuk13, Takahashi Yutaka1, Jou Shiann-Tarrng1, Feng Jian1, Nakajima Hideaki1, Ihle James N.14
Affiliation:
1. Department of Biochemistry 2. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724 3. Department of Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38105 4. Howard Hughes Medical Institute, St. Jude Children's Research Hospital
Abstract
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.
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
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