Regulation of Lck activity by CD4 and CD28 in the immunological synapse View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-03

AUTHORS

Amy D. Holdorf, Kyeong-Hee Lee, W. Richard Burack, Paul M. Allen, Andrey S. Shaw

ABSTRACT

Although the Src family tyrosine kinase Lck is essential for T cell receptor (TCR) signaling, whether or how Lck is activated is unknown. Using a phosphospecific antiserum to Lck, we show here that Lck becomes autophosphorylated when T cells are stimulated by antigen-presenting cells (APCs). We found that TCR cross-linking alone could not stimulate Lck autophosphorylation and CD45 was not required for this process. Instead, the T cell accessory molecules CD4 and CD28 cooperated to induce autophosphorylation of Lck. CD4 recruited Lck to the T cell--APC interface, whereas CD28 sustained Lck activation. These data show how the multiple interactions afforded by the immunological synapse drive efficient and highly specific signaling. More... »

PAGES

259-264

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ni761

DOI

http://dx.doi.org/10.1038/ni761

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002992988

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11828322


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