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Beta 1 integrin-mediated signaling in human T cells
1Institute of Medical Science, University of Tokyo, Japan.
Human Cell
|September 1, 1996
Summary
Beta 1 integrin engagement triggers tyrosine phosphorylation in T lymphocytes. A novel protein, Cas-L, was identified as a key player in this signaling pathway, interacting with FAK and downstream effectors.
Area of Science:
- Cell Biology
- Molecular Biology
- Immunology
Background:
- Beta 1 integrin engagement initiates protein tyrosine phosphorylation in T lymphocytes.
- Previous studies identified several tyrosine-phosphorylated proteins, but a 105 KD protein (pp105) remained uncharacterized.
Purpose of the Study:
- To identify the novel 105 KD tyrosine-phosphorylated protein (pp105) in T lymphocytes.
- To elucidate the role of pp105 in beta 1 integrin signaling.
Main Methods:
- Protein identification and characterization.
- Analysis of protein-protein interactions using co-immunoprecipitation.
- Investigation of signaling pathways through tyrosine phosphorylation assays.
Main Results:
- The 105 KD tyrosine-phosphorylated protein (pp105) was identified as a novel p130Cas related protein, designated Cas-L (lymphocyte type Cas).
- Cas-L is preferentially expressed in lymphoid cells and associates with the FAK C-terminal region upon integrin stimulation.
- Tyrosine phosphorylated Cas-L binds to SH2 domains of Crk, Nck, and SHPTP2.
Conclusions:
- Cas-L represents a novel component of the beta 1 integrin signaling pathway in T lymphocytes.
- The findings reveal a new architecture of beta 1 integrin-mediated protein tyrosine phosphorylation.
- Crk, Nck, and SHPTP2 are implicated in the downstream signaling of beta 1 integrin activation.