HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 8, 6012-6017, February 21, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/8/6012    most recent M207942200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sakakibara, A. Articles by Katagiri, T. Search for Related Content PubMed PubMed Citation Articles by Sakakibara, A. Articles by Katagiri, T. Social Bookmarking                      What's this?

A Novel Hematopoietic Adaptor Protein, Chat-H, Positively Regulates T Cell Receptor-mediated Interleukin-2 Production by Jurkat Cells^*

Akira Sakakibara^§¶, Seisuke Hattori^**, Shun Nakamura, and Takuya Katagiri^¶**

From the  Division of Biochemistry and Cellular Biology, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Kodaira, Tokyo 187-8502, Japan, the ^§ Department of Cell Biology, University of Virginia, Charlottesville, Virginia 22908, and the  Division of Cellular Proteomics, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan

Chat (Cas/HEF1-associated signal transducer) is a novel adaptor protein with an N-terminal Src homology-2 domain and C-terminal Cas/HEF1 association domain. We report here the molecular cloning of Chat-H, the hematopoietic isoform of Chat. Chat-H has an extended N-terminal domain besides the known Chat domain structures, suggesting a unique function of Chat-H in hematopoietic cells. Jurkat transfectants overexpressing Chat-H show a marked increase in interleukin-2 production after costimulation of T cell receptor and CD28. The degree of JNK activation is enhanced substantially in the Chat-H transfectants upon costimulation. The Src homology-2 domain mutant of Chat-H loses this signal modulating activity. Expression of the Cas/HEF1 association domain mutant exhibits a dominant negative effect on both JNK activation and interleukin-2 production. We further found that Chat-H forms a complex with Pyk2H and enhances its tyrosine 402 phosphorylation, an up-regulator of the JNK pathway. These results suggest that Chat-H positively controls T cell function via integrating the costimulatory signals.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AB043953.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				C. Giallourakis, Z. Cao, T. Green, H. Wachtel, X. Xie, M. Lopez-Illasaca, M. Daly, J. Rioux, and R. Xavier A molecular-properties-based approach to understanding PDZ domain proteins and PDZ ligands Genome Res., August 1, 2006; 16(8): 1056 - 1072. [Abstract] [Full Text] [PDF]

				M. Dail, M. S. Kalo, J. A. Seddon, J.-F. Cote, K. Vuori, and E. B. Pasquale SHEP1 Function in Cell Migration Is Impaired by a Single Amino Acid Mutation That Disrupts Association with the Scaffolding Protein Cas but Not with Ras GTPases J. Biol. Chem., October 1, 2004; 279(40): 41892 - 41902. [Abstract] [Full Text] [PDF]