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Rho effectors and reorganization of actin cytoskeleton
Author(s) -
Narumiya Shuh,
Ishizaki Toshimasa,
Watanabe Naoki
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00317-7
Subject(s) - microbiology and biotechnology , profilin , cytoskeleton , mdia1 , actin , cytokinesis , actin cytoskeleton , actin remodeling , myosin , focal adhesion , actin binding protein , rac gtp binding proteins , formins , chemistry , biology , rac1 , biochemistry , cell , cell division , signal transduction
The small GTPase Rho regulates several actomyosin‐based cellular processes such as cell adhesion, cytokinesis and contraction. The biochemical mechanisms of these actions remain unknown. Recently, several GTP‐Rho binding proteins were isolated. Among them, p140mDia and p160ROCK appear to work as Rho effectors mediating its action on the cytoskeleton. p140mDia induces actin polymerization by recruiting an actin binding protein, profilin, to the site of Rho action. p160ROCK induces focal adhesions and stress fibers by activating integrin and clustering them by the use of myosin‐based contractility.