Evidence map›Paper›PMID 20533885›Full record

ReviewAnnual review of biochemistry2010

Physical mechanisms of signal integration by WASP family proteins.

Shae B Padrick, Michael K Rosen

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed
16.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

160 citing papers in PubMed, 260 citations in OpenAlex.

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  8. Electrical Forces Improve Memory in Old Age.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
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  13. Structural basis for coupling of the WASH subunit FAM21 with the endosomal SNX27-Retromer complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. mBio · 2024
    Article
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100 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Shae B PadrickHoward Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA. Shae.Padrick@UTSouthwestern.edu
Michael K Rosen
Howard Hughes Medical Institute · USThe University of Texas Southwestern Medical Center · US

Funding

STRUCTURAL STUDY OF RHO-GTPASE REGULATORS AND EFFECTORSR01GM056322 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ROSEN, MICHAEL K · 1997 to 2019
$5.7M
Inhibition of Scar by the HEM2/Abi2/Pir121 ComplexF32GM069179 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI PADRICK, SHAE B · 2003 to 2005
$131k
Howard Hughes Medical InstituteNIGMS NIH HHS 1F32-GM06917902NIGMS NIH HHS F32 GM069179NIGMS NIH HHS R01 GM056322NIGMS NIH HHS R01-GM56322
6 · The paper itself

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-VCA 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.

Indexed as

Actin-Related Protein 2-3 ComplexAllosteric RegulationHumansProtein MultimerizationProtein Structure, TertiarySignal TransductionWiskott-Aldrich Syndrome Protein FamilyActin-Related Protein 2-3 ComplexWiskott-Aldrich Syndrome Protein Family

Identifiers

PMID20533885
PMCPMC3017724
OpenAlexW1997228602

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.