Tyrosine phosphorylation of VHR phosphatase by ZAP-70 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-11-25

AUTHORS

Andres Alonso, Souad Rahmouni, Scott Williams, Marianne van Stipdonk, Lukasz Jaroszewski, Adam Godzik, Robert T. Abraham, Stephen P. Schoenberger, Tomas Mustelin

ABSTRACT

The ZAP-70 tyrosine kinase is a key component of the signaling machinery for the T cell antigen receptor (TCR). Whereas recruitment and activation of ZAP-70 are relatively well understood, the proteins phosphorylated by ZAP-70 are incompletely known. We report here that VHR, a Vaccinia virus VH1-related dual-specific protein phosphatase that inactivates the mitogen-activated kinases Erk2 and Jnk, is phosphorylated at Y138 by ZAP-70. Tyr138 phosphorylation was required for VHR to inhibit the Erk2–Elk-1 pathway and, conversely, the VHRY138F mutant augmented TCR-induced Erk2 kinase and activation of the gene encoding interleukin 2. These results suggest that VHR is a target for ZAP-70 and tempers activation of the Erk2 pathway in a ZAP-70–controlled manner. More... »

PAGES

44-48

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ni856

DOI

http://dx.doi.org/10.1038/ni856

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036618205

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12447358


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