Rac regulates phosphorylation of the myosin-II heavy chain, actinomyosin disassembly and cell spreading.
Publication year
1999Source
Nat Cell Biol, 1, 4, (1999), pp. 242-8Publication type
Article / Letter to editor
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Organization
Tumorimmunology
Journal title
Nat Cell Biol
Volume
vol. 1
Issue
iss. 4
Page start
p. 242
Page end
p. 8
Subject
TumorimmunologyAbstract
GTPases of the Rho family regulate actinomyosin-based contraction in non-muscle cells. Activation of Rho increases contractility, leading to cell rounding and neurite retraction in neuronal cell lines. Activation of Rac promotes cell spreading and interferes with Rho-mediated cell rounding. Here we show that activation of Rac may antagonize Rho by regulating phosphorylation of the myosin-II heavy chain. Stimulation of PC12 cells or N1E-115 neuroblastoma cells with bradykinin induces phosphorylation of threonine residues in the myosin-II heavy chain; this phosphorylation is Ca2+ dependent and regulated by Rac. Both bradykinin-mediated and constitutive activation of Rac promote cell spreading, accompanied by a loss of cortical myosin II. Our results identify the myosin-II heavy chain as a new target of Rac-regulated kinase pathways, and implicate Rac as a Rho antagonist during myosin-II-dependent cell-shape changes.
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- Academic publications [245050]
- Faculty of Medical Sciences [93209]
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