Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 79
Volume 79, Issue -, Pages 707-735Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biochem.77.060407.135452
Keywords
actin regulation; allostery; Arp2/3 complex; Rho GTPase; signal transduction
Categories
Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [F32 GM069179, R01 GM056322-15, R01-GM56322, 1F32-GM06917902, F32 GM069179-03, R01 GM056322] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [F32GM069179, R01GM056322] Funding Source: NIH RePORTER
Ask authors/readers for more resources
The proteins of the Wiskott-Aldrich syndrome protein (WASP) family are activators of the ubiquitous actin nucleation factor, the Arp2/3 complex. WASP family proteins contain a C-terminal VCA domain that binds and activates the Arp2/3 complex in response to numerous inputs, including Rho family GTPases, phosphoinositide lipids, SH3 domain containing proteins, kinases, and phosphatases. In the archetypal members of the family, WASP and N-WASP, these signals are integrated through two levels of regulation, an allosteric autoinhibitory interaction, in which the VCA is sequestered from the Arp2/3 complex, and dimerization/oligomerization, in which multi-VGA complexes are better activators of the Arp2/3 complex than monomers. Here, we review the structural, biochemical, and biophysical details of these mechanisms and illustrate how they work together to control WASP activity in response to multiple inputs. These regulatory principles, derived from studies of WASP and N-WASP, are likely to apply broadly across the family.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available