Tyrosine 192 within the SH2 domain of the Src-protein tyrosine kinase p56^Lck regulates T-cell activation independently of Lck/CD45 interactions.

ABSTRACT:

Background

Upon engagement of the T-cell receptor (TCR), the Src-family protein tyrosine kinase p56Lck phosphorylates components of the TCR (e.g. the TCRζ chains), thereby initiating T-cell activation. The enzymatic activity of Lck is primarily regulated via reversible and dynamic phosphorylation of two tyrosine residues, Y394 and Y505. Lck possesses an additional highly conserved tyrosine Y192, located within the SH2 domain, whose role in T-cell activation is not fully understood.

Methods

Knock-in mice expressing a phospho-mimetic (Y192E) form of Lck were generated. Cellular and biochemical characterization was performed to elucidate the function of Y192 in primary T cells. HEK 293T and Jurkat T cells were used for in vitro studies.

Results

Co-immunoprecipitation stu

SUBMITTER: Kastle M 

PROVIDER: S-EPMC7682018 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature