Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes.
Adapter molecule crk
DOI:
10.1084/jem.184.4.1365
Publication Date:
2004-06-24T07:56:10Z
AUTHORS (6)
ABSTRACT
Integrin/ligand binding evokes tyrosine phosphorylation of various proteins. We reported previously that a 105 kD protein (pp105) was phosphorylated by the engagement beta 1 integrins in T lymphocytes. show here pp105 is novel p130Cas (Crk-associated substrate)-related protein. Deduced amino acid sequence revealed contains conserved motifs with p130Cas, and both bind to focal adhesion kinase (pp125FAK) Crk. However, has clearly distinct structure from preferentially expressed lymphocytes, whereas adherent cells. With these findings, we designate as Cas-L, lymphocyte-type Cas. Furthermore, demonstrate integrin/ligand results recruitment Crk, Nck, SHPTP2 pp105. These findings further define roles pp105/Cas-L pp125FAK integrin-mediated signaling pathways.
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