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Phosphorylation of G Protein–Coupled Receptor Kinase 2–Interacting Protein 1 Tyrosine 392 Is Required for Phospholipase C-γ Activation and Podosome Formation in Vascular Smooth Muscle Cells
Author(s) -
Jing Wang,
Guoyong Yin,
Prashanthi Me,
Jinjiang Pang,
Elaine M. Smolock,
Chen Yan,
Bradford C. Berk
Publication year - 2010
Publication title -
arteriosclerosis thrombosis and vascular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.007
H-Index - 270
eISSN - 1524-4636
pISSN - 1079-5642
DOI - 10.1161/atvbaha.110.212415
Subject(s) - phosphorylation , podosome , microbiology and biotechnology , receptor tyrosine kinase , proto oncogene tyrosine protein kinase src , tyrosine phosphorylation , chemistry , vascular smooth muscle , biochemistry , smooth muscle , biology , endocrinology , cell , cytoskeleton
Podosomes, which are actin-rich structures, contribute to cell motility, matrix remodeling, and tissue remodeling. We have shown that G protein-coupled receptor kinase 2-interacting protein 1 (GIT1) colocalizes with podosomes and is important in podosome formation in endothelial cells. Src stimulates GIT1 tyrosine phosphorylation, which is critical for phospholipase C-γ (PLCγ) activation. In this study, we identified specific GIT1 tyrosines required for PLCγ activation and podosome formation in vascular smooth muscle cells (VSMC).

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