Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Pak1 regulates focal adhesion strength, myosin IIA distribution, and actin dynamics to optimize cell migration

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Delorme-Walker, V. D.
  • Peterson, J. R.
  • Chernoff, J.
  • Waterman, C. M.
  • Danuser, G.
  • DerMardirossian, Celine
  • Bokoch, G. M.

publication date

  • June 2011

journal

  • Journal of Cell Biology  Journal

abstract

  • Cell motility requires the spatial and temporal coordination of forces in the actomyosin cytoskeleton with extracellular adhesion. The biochemical mechanism that coordinates filamentous actin (F-actin) assembly, myosin contractility, adhesion dynamics, and motility to maintain the balance between adhesion and contraction remains unknown. In this paper, we show that p21-activated kinases (Paks), downstream effectors of the small guanosine triphosphatases Rac and Cdc42, biochemically couple leading-edge actin dynamics to focal adhesion (FA) dynamics. Quantitative live cell microscopy assays revealed that the inhibition of Paks abolished F-actin flow in the lamella, displaced myosin IIA from the cell edge, and decreased FA turnover. We show that, by controlling the dynamics of these three systems, Paks regulate the protrusive activity and migration of epithelial cells. Furthermore, we found that expressing Pak1 was sufficient to overcome the inhibitory effects of excess adhesion strength on cell motility. These findings establish Paks as critical molecules coordinating cytoskeletal systems for efficient cell migration.

subject areas

  • Actins
  • Animals
  • Cell Adhesion
  • Cell Movement
  • Extracellular Matrix
  • Kinetics
  • Nonmuscle Myosin Type IIA
  • Paxillin
  • Phenotype
  • Potoroidae
  • p21-Activated Kinases
scroll to property group menus

Identity

PubMed Central ID

  • PMC3216326

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.201010059

PubMed ID

  • 21708980
scroll to property group menus

Additional Document Info

start page

  • 1289

end page

  • 1303

volume

  • 193

issue

  • 7

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support