Abstract
Recent genetic evidence demonstrated that Shc is a critical molecule for T cell activation and differentiation. However, how Shc is coupled to the T cell antigen receptor (TCR) has not been clearly characterized. Here we report that the tyrosine kinase Lck functions as a connecting molecule for TCR and Shc. Lck plays a critical role in TCR signal transduction by phosphorylating the immuno-receptor tyrosine based activation motif (ITAM). Our data shows that the PTB domain of Shc binds the SH2/3 domains of Lck in a phosphotyrosine-independent manner. Inhibition of the Lck/Shc interaction led to the loss of IL-2 promoter activation, confirming that the role of Shc in IL-2 production requires its interaction with Lck. Together, the data show that Shc is connected to the activated TCR via direct interaction with Lck.
Original language | English (US) |
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Pages (from-to) | 1182-1189 |
Number of pages | 8 |
Journal | Cellular Signalling |
Volume | 18 |
Issue number | 8 |
DOIs | |
State | Published - Aug 1 2006 |
Keywords
- LAT
- Lck
- PTB
- SH2
- SH3
- Shc
- TCR
- ZAP-70
ASJC Scopus subject areas
- Cell Biology