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Book chapter
Physical Mechanisms of Signal Integration by WASP Family Proteins
Annual Review of Biochemistry, pp 707-735
01 Jan 2010
PMID: 20533885
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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.
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Details
- Title
- Physical Mechanisms of Signal Integration by WASP Family Proteins
- Creators
- Shae B. Padrick - Howard Hughes Medical InstituteMichael K. Rosen - Applied BioPhysics (United States)
- Contributors
- R D Kornberg (Editor)CRH Raetz (Editor)J E Rothman (Editor)J W Thorner (Editor)
- Publication Details
- Annual Review of Biochemistry, pp 707-735
- Series
- Annual Review of Biochemistry
- Publisher
- Annual Reviews; PALO ALTO
- Number of pages
- 29
- Grant note
- Howard Hughes Medical Institute R01 GM056322; F32 GM069179-03; R01-GM56322; F32 GM069179; R01 GM056322-15; 1F32-GM06917902 / NIGMS NIH HHS; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS) R01GM056322 / NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS)
- Resource Type
- Book chapter
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000280225300025
- Scopus ID
- 2-s2.0-77953637330
- Other Identifier
- 991020836321704721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology