1. SNARE-mediated membrane traffic modulates RhoA-regulated focal adhesion formation
- Author
-
Marc G. Coppolino, Michael Skalski, Eva M. Gonon, and Michelle J. Kean
- Subjects
rac1 GTP-Binding Protein ,RHOA ,Pyridines ,Biophysics ,CHO Cells ,Protein Serine-Threonine Kinases ,Biochemistry ,Focal adhesion ,03 medical and health sciences ,Cricetulus ,0302 clinical medicine ,Tetanus Toxin ,Cell Movement ,Structural Biology ,Cricetinae ,Stress Fibers ,Genetics ,Animals ,N-ethylmaleimide sensitive fusion protein ,Cell adhesion ,N-Ethylmaleimide-Sensitive Proteins ,Molecular Biology ,030304 developmental biology ,Focal Adhesions ,rho-Associated Kinases ,0303 health sciences ,biology ,Cell Membrane ,Soluble NSF attachment protein receptor ,Intracellular Signaling Peptides and Proteins ,Biological Transport ,RhoA ,Cell Biology ,Transfection ,Amides ,Membrane traffic ,Cell biology ,Protein Transport ,Vesicle-associated membrane protein ,biology.protein ,Soluble NSF attachment protein ,Lamellipodium ,SNARE Proteins ,rhoA GTP-Binding Protein ,030217 neurology & neurosurgery - Abstract
In the present study, we examined the role of soluble NSF attachment protein receptor (SNARE)-mediated membrane traffic in the formation of focal adhesions during cell spreading. CHO-K1 cells expressing a dominant-negative form of N-ethylmaleimide-sensitive factor (E329Q-NSF) were unable to spread as well as control cells and they formed focal adhesions (FAs) that were larger than those in control cells. FA formation was impaired in cells transfected with a dominant-negative form of RhoA, but, significantly, not in cells simultaneously expressing dominant-negative NSF. Treatment of E329Q-NSF-expressing cells with the ROCK inhibitor Y-27632 did inhibit FA formation. The results are consistent with a model of cell adhesion in which SNARE-mediated membrane traffic is required for both the elaboration of lamellipodia and the modulation of biochemical signals that control RhoA-mediated FA assembly.
- Published
- 2005