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Rho effectors and reorganization of actin cytoskeleton
- Source :
- FEBS Letters. 410:68-72
- Publication Year :
- 1997
- Publisher :
- Wiley, 1997.
-
Abstract
- 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.
- Subjects :
- Stress fiber
Biophysics
Arp2/3 complex
macromolecular substances
Protein Serine-Threonine Kinases
Contractility
Models, Biological
Biochemistry
GTP-Binding Proteins
Structural Biology
Genetics
Actin polymerization
Animals
Actin-binding protein
rhoB GTP-Binding Protein
Molecular Biology
Rho-associated protein kinase
rho-Associated Kinases
biology
Chemistry
Rho GTPase
Intracellular Signaling Peptides and Proteins
Cell adhesion
Membrane Proteins
Actin remodeling
Cell Biology
Actin cytoskeleton
Actins
Cell biology
Focal adhesion
Profilin
biology.protein
MDia1
Carrier Proteins
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 410
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....95ee4db63a5287d790cc6893bf9dab06