Document Detail

The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402 and 580 occurs via a distinct mechanism than other receptor systems.
MedLine Citation:
PMID:  20028775     Owner:  NLM     Status:  MEDLINE    
The tyrosine kinase Pyk2 is vital for integrating receptor-mediated signals controlling adhesion and motility in neuronal, epithelial, and hematopoietic cell types. In T cells, the stimulation of the TCR and costimulatory, chemokine, cytokine, and integrin receptors leads to the phosphorylation of Pyk2 and the induction of its catalytic activity. However, our understanding of the mechanism of the TCR-induced, site-specific phosphorylation of this kinase is incomplete and contradictory. To address this issue, the role of individual signaling pathways in the phosphorylation of Pyk2 tyrosines 402 and 580 upon TCR activation was assessed in human T cells. In contrast to other receptor systems, the TCR-induced phosphorylation of Pyk2 tyrosines 402 and 580 was dependent on the Src family kinases, Fyn or Lck. Interestingly, the TCR-mediated phosphorylation of Pyk2 tyrosines 402 and 580 did not require Ca(2+) influx, ZAP-70 activation, actin cytoskeleton rearrangement, or PI3K function. These observations are different than other receptor systems, which require the induction of one or more of these pathways. Together, these data have defined more fully the mechanism for the TCR-induced phosphorylation of specific sites on Pyk2, suggesting that the TCR has a distinct pathway for the activation of Pyk2 compared with other receptor systems.
Michaela Collins; Mikaela Tremblay; Nicole Chapman; Miranda Curtiss; Paul B Rothman; Jon C D Houtman
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-12-22
Journal Detail:
Title:  Journal of leukocyte biology     Volume:  87     ISSN:  1938-3673     ISO Abbreviation:  J. Leukoc. Biol.     Publication Date:  2010 Apr 
Date Detail:
Created Date:  2010-04-01     Completed Date:  2010-04-27     Revised Date:  2012-06-05    
Medline Journal Info:
Nlm Unique ID:  8405628     Medline TA:  J Leukoc Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  691-701     Citation Subset:  IM    
Department of Microbiology, Carver College of Medicine, University of Iowa, 2210 MERF, Iowa City, IA 52242, USA.
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MeSH Terms
Calcium / immunology,  metabolism
Cell Adhesion / immunology
Enzyme Activation / immunology
Focal Adhesion Kinase 2 / immunology,  metabolism*
Jurkat Cells
Lymphocyte Specific Protein Tyrosine Kinase p56(lck) / immunology,  metabolism
Phosphorylation / immunology
Proto-Oncogene Proteins c-fyn / immunology,  metabolism
Receptors, Antigen, T-Cell / immunology,  metabolism*
T-Lymphocytes / enzymology*,  immunology
Tyrosine / immunology,  metabolism*
ZAP-70 Protein-Tyrosine Kinase / immunology,  metabolism
Reg. No./Substance:
0/Receptors, Antigen, T-Cell; 55520-40-6/Tyrosine; 7440-70-2/Calcium; EC 2.7.1.-/PTK2B protein, human; EC Adhesion Kinase 2; EC protein, human; EC Specific Protein Tyrosine Kinase p56(lck); EC Proteins c-fyn; EC Protein-Tyrosine Kinase; EC protein, human

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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