This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Carpino, N.
Right arrow Articles by Ihle, J. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Carpino, N.
Right arrow Articles by Ihle, J. N.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2002, p. 7491-7500, Vol. 22, No. 21
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.21.7491-7500.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification, cDNA Cloning, and Targeted Deletion of p70, a Novel, Ubiquitously Expressed SH3 Domain-Containing Protein

Nick Carpino,1 Ryuji Kobayashi,2,{dagger} Heesuk Zang,1,3 Yutaka Takahashi,1 Shiann-Tarrng Jou,1,{ddagger} Jian Feng,1 Hideaki Nakajima,1,3 and James N. Ihle1,4*

Department of Biochemistry,1 Howard Hughes Medical Institute, St. Jude Children's Research Hospital,4 Department of Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38105,3 Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 117242

Received 7 May 2002/ Returned for modification 15 July 2002/ Accepted 2 August 2002

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.

* Corresponding author. Mailing address: Howard Hughes Medical Institute, St. Jude Children's Research Hospital, Memphis, TN 38105. Phone: (901) 495-3422. Fax: (901) 525-8025. E-mail: james.ihle{at}stjude.org.

{dagger} Present address: Department of Molecular Pathology, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030.

{ddagger} Present address: Department of Pediatrics, National Taiwan University Hospital, Taipei 100, Taiwan.

§ Present address: Division of Cellular Therapy, The Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan.

Molecular and Cellular Biology, November 2002, p. 7491-7500, Vol. 22, No. 21
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.21.7491-7500.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Brehme, M., Hantschel, O., Colinge, J., Kaupe, I., Planyavsky, M., Kocher, T., Mechtler, K., Bennett, K. L., Superti-Furga, G. (2009). Charting the molecular network of the drug target Bcr-Abl. Proc. Natl. Acad. Sci. USA 106: 7414-7419 [Abstract] [Full Text]  
  • Cheng, H., Ross, J. A., Frost, J. A., Kirken, R. A. (2008). Phosphorylation of Human Jak3 at Tyrosines 904 and 939 Positively Regulates Its Activity. Mol. Cell. Biol. 28: 2271-2282 [Abstract] [Full Text]  
  • Collingwood, T. S., Smirnova, E. V., Bogush, M., Carpino, N., Annan, R. S., Tsygankov, A. Y. (2007). T-cell Ubiquitin Ligand Affects Cell Death through a Functional Interaction with Apoptosis-inducing Factor, a Key Factor of Caspase-independent Apoptosis. J. Biol. Chem. 282: 30920-30928 [Abstract] [Full Text]  
  • Lo, S.-C., Hannink, M. (2006). PGAM5, a Bcl-XL-interacting Protein, Is a Novel Substrate for the Redox-regulated Keap1-dependent Ubiquitin Ligase Complex. J. Biol. Chem. 281: 37893-37903 [Abstract] [Full Text]  
  • Mazurkiewicz-Munoz, A. M., Argetsinger, L. S., Kouadio, J.-L. K., Stensballe, A., Jensen, O. N., Cline, J. M., Carter-Su, C. (2006). Phosphorylation of JAK2 at Serine 523: a Negative Regulator of JAK2 That Is Stimulated by Growth Hormone and Epidermal Growth Factor.. Mol. Cell. Biol. 26: 4052-4062 [Abstract] [Full Text]  
  • Kowanetz, K., Crosetto, N., Haglund, K., Schmidt, M. H. H., Heldin, C.-H., Dikic, I. (2004). Suppressors of T-cell Receptor Signaling Sts-1 and Sts-2 Bind to Cbl and Inhibit Endocytosis of Receptor Tyrosine Kinases. J. Biol. Chem. 279: 32786-32795 [Abstract] [Full Text]  
  • Argetsinger, L. S., Kouadio, J.-L. K., Steen, H., Stensballe, A., Jensen, O. N., Carter-Su, C. (2004). Autophosphorylation of JAK2 on Tyrosines 221 and 570 Regulates Its Activity. Mol. Cell. Biol. 24: 4955-4967 [Abstract] [Full Text]  
  • Feener, E. P., Rosario, F., Dunn, S. L., Stancheva, Z., Myers, M. G. Jr. (2004). Tyrosine Phosphorylation of Jak2 in the JH2 Domain Inhibits Cytokine Signaling. Mol. Cell. Biol. 24: 4968-4978 [Abstract] [Full Text]  
  • Kurzer, J. H., Argetsinger, L. S., Zhou, Y.-J., Kouadio, J.-L. K., O'Shea, J. J., Carter-Su, C. (2004). Tyrosine 813 Is a Site of JAK2 Autophosphorylation Critical for Activation of JAK2 by SH2-B{beta}. Mol. Cell. Biol. 24: 4557-4570 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»