Microtubule depolymerization induces stress fibers, focal adhesions, and DNA synthesis via the GTP-binding protein Rho. Cell Adhes Commun 1998 Jun;5(4):249-55
Date
10/08/1998Pubmed ID
9762466DOI
10.3109/15419069809040295Scopus ID
2-s2.0-0032454273 (requires institutional sign-in at Scopus site) 179 CitationsAbstract
Microtubule depolymerization has multiple consequences that include actin stress fiber and focal adhesion assembly, increased tyrosine phosphorylation and DNA synthesis. Similar effects induced by serum, or agents such as lysophosphatidic acid, have previously been shown to be mediated by the GTP-binding protein Rho. We have investigated whether the effects of microtubule depolymerization are similarly mediated by Rho and show that they are blocked by the specific Rho inhibitor, C3 transferase. Because microtubule depolymerization induces these effects in quiescent cells, in which Rho is largely inactive, we conclude that microtubule depolymerization leads to activation of Rho. The activation of Rho in response to microtubule depolymerization and the consequent stimulation of contractility suggest a mechanism by which microtubules may regulate microfilament function in various motile phenomena. These range from growth cone extension to the development of the contractile ring during cytokinesis, in which there are interactions between the microtubule and microfilament systems.
Author List
Liu BP, Chrzanowska-Wodnicka M, Burridge KAuthor
Magdalena Chrzanowska PhD Professor in the Pharmacology and Toxicology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
3T3 CellsActin Cytoskeleton
Animals
Antineoplastic Agents
Cell Adhesion
Cell Cycle
Culture Media, Serum-Free
Cytoskeleton
DNA
GTP Phosphohydrolases
GTP-Binding Proteins
Mice
Mice, Inbred BALB C
Microtubules
Nocodazole
Polymers
Stress, Mechanical
rho GTP-Binding Proteins
