Src-dependent phosphorylation of ROCK participates in regulation of focal adhesion dynamics.

Article Details

Citation

Lee HH, Tien SC, Jou TS, Chang YC, Jhong JG, Chang ZF

Src-dependent phosphorylation of ROCK participates in regulation of focal adhesion dynamics.

J Cell Sci. 2010 Oct 1;123(Pt 19):3368-77. doi: 10.1242/jcs.071555. Epub 2010 Sep 7.

PubMed ID
20826462 [ View in PubMed
]
Abstract

When a cell migrates, the RhoA-ROCK-mediated contractile signal is suppressed in the leading edge to allow dynamic adhesions for protrusion. However, several studies have reported that RhoA is indeed active in the leading edge of a migrating cell during serum stimulation. Here, we present evidence that regulation of ROCKII phosphorylation at the Y722 site in peripheral focal contacts is crucial for controlling the turnover of the focal adhesion (FA) complex uncoupled from RhoA activation during serum-stimulated migration. However, this phosphorylation control is dispensable for migration when RhoA is downregulated in cells treated with platelet-derived growth factor (PDGF). We further present evidence that ROCKII is phosphorylated by Src in FAs and this phosphorylation event decreases RhoA binding activity of ROCKII. Lack of this regulatory control leads to sustained myosin-mediated contractility and FA elongation during lysophosphatidic acid (LPA) stimulation. Altogether, our data suggest that Src-dependent ROCKII phosphorylation provides a means of tuning contractility required for FAs dynamics when RhoA is active.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Rho-associated protein kinase 2O75116Details