Evidence map›Paper›PMID 20169536›Full record

ArticleCytoskeleton (Hoboken, N.J.)2010

A central role for the WH2 domain of Srv2/CAP in recharging actin monomers to drive actin turnover in vitro and in vivo.

Faisal Chaudhry, Kristin Little, Lou Talarico, Omar Quintero-Monzon, Bruce L Goode

Abstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

43 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Article
  15. Regulation of INF2-mediated actin polymerization through site-specific lysine acetylation of actin itself.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Review
  17. Article
  18. Article
  19. Mechanism of CAP1-mediated apical actin polymerization in pollen tubes.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Review
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

5 authors at 1 institution in 1 country.

Faisal ChaudhryDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, Massachusetts, USA.
Kristin Little
Lou Talarico
Omar Quintero-Monzon
Bruce L Goode
Brandeis University · US

Funding

MECHNISMS REGULATING ACTIN ASSEMBLYR01GM063691 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2002 to 2019
$7.5M
Macromolecular Structure MechanismT32GM007596 · NIGMS · BRANDEIS UNIVERSITY · PI OPRIAN, DANIEL D · 1985 to 2019
$4.5M
Regulation of formins and cell polarity in yeastR01GM083137 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2008 to 2019
$4.3M
NIGMS NIH HHS GM083137NIGMS NIH HHS GM63691NIGMS NIH HHS R01 GM063691NIGMS NIH HHS R01 GM083137NIGMS NIH HHS T32 GM007596
6 · The paper itself

Abstract

Cellular processes propelled by actin polymerization require rapid disassembly of filaments, and then efficient recycling of ADF/cofilin-bound ADP-actin monomers back to an assembly-competent ATP-bound state. How monomer recharging is regulated in vivo is still not well understood, but recent work suggests the involvement of the ubiquitous actin-monomer binding protein Srv2/CAP. To better understand Srv2/CAP mechanism, we explored the contribution of its WH2 domain, the function of which has remained highly elusive. We found that the WH2 domain binds to actin monomers and, unlike most other WH2 domains, exhibits similar binding affinity for ATP-actin and ADP-actin (K(d) approximately 1.5 microM). Mutations in the WH2 domain that impair actin binding disrupt the ability of purified full-length Srv2/CAP to catalyze nucleotide exchange on ADF/cofilin-bound actin monomers and accelerate actin turnover in vitro. The same mutations impair Srv2/CAP function in vivo in regulating actin organization, cell growth, and cell morphogenesis. Thus, normal cell growth and organization depend on the ability of Srv2/CAP to recharge actin monomers, and the WH2 domain plays a central role in this process. Our data also reveal that while most isolated WH2 domains inhibit nucleotide exchange on actin, WH2 domains in the context of intact proteins can help promote nucleotide exchange.

Indexed as

ActinsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCytoskeletal ProteinsDNA Mutational AnalysisMicroscopy, FluorescenceMolecular Sequence DataProtein BindingProtein Structure, TertiaryRabbitsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidActinsAdaptor Proteins, Signal TransducingCytoskeletal ProteinsSaccharomyces cerevisiae ProteinsSRV2 protein, S cerevisiae

Identifiers

PMID20169536
PMCPMC2857556
OpenAlexW2062796609

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.