Evidence map›Paper›PMID 19201756›Full record

ArticleThe Journal of biological chemistry2009

Reconstitution and dissection of the 600-kDa Srv2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover.

Omar Quintero-Monzon, Erin M Jonasson, Enni Bertling, Lou Talarico, Faisal Chaudhry, Maarit Sihvo, Pekka Lappalainen, Bruce L Goode

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
–field-weighted citation impact
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

44 citing papers in PubMed.

  1. Article
  2. Article
  3. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. CAP1 binds and activates adenylyl cyclase in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Review
  11. 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
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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
  18. Review
  19. Article
  20. Article
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

8 authors.

Omar Quintero-MonzonDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, Massachusetts 02454, USA.
Erin M Jonasson
Enni Bertling
Lou Talarico
Faisal Chaudhry
Maarit Sihvo
Pekka Lappalainen
Bruce L Goode

Funding

MECHNISMS REGULATING ACTIN ASSEMBLYR01GM063691 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2002 to 2019
$7.5M
GENETIC AND BIOCHEMICAL MECHANISMS OF REGULATIONT32GM007122 · NIGMS · BRANDEIS UNIVERSITY · PI LOVETT, SUSAN THOMAS · 1985 to 2020
$7.5M
Macromolecular Structure MechanismT32GM007596 · NIGMS · BRANDEIS UNIVERSITY · PI OPRIAN, DANIEL D · 1985 to 2019
$4.5M
NIGMS NIH HHS GM63691NIGMS NIH HHS R01 GM063691NIGMS NIH HHS T32 GM007122NIGMS NIH HHS T32 GM007596
6 · The paper itself

Abstract

Srv2/cyclase-associated protein is expressed in virtually all plant, animal, and fungal organisms and has a conserved role in promoting actin depolymerizing factor/cofilin-mediated actin turnover. This is achieved by the abilities of Srv2 to recycle cofilin from ADP-actin monomers and to promote nucleotide exchange (ATP for ADP) on actin monomers. Despite this important and universal role in facilitating actin turnover, the mechanism underlying Srv2 function has remained elusive. Previous studies have demonstrated a critical functional role for the G-actin-binding C-terminal half of Srv2. Here we describe an equally important role in vivo for the N-terminal half of Srv2 in driving actin turnover. We pinpoint this activity to a conserved patch of surface residues on the N-terminal dimeric helical folded domain of Srv2, and we show that this functional site interacts with cofilin-actin complexes. Furthermore, we show that this site is essential for Srv2 acceleration of cofilin-mediated actin turnover in vitro. A cognate Srv2-binding site is identified on a conserved surface of cofilin, suggesting that this function likely extends to other organisms. In addition, our analyses reveal that higher order oligomerization of Srv2 depends on its N-terminal predicted coiled coil domain and that oligomerization optimizes Srv2 function in vitro and in vivo. Based on these data, we present a revised model for the mechanism by which Srv2 promotes actin turnover, in which coordinated activities of its N- and C-terminal halves catalyze sequential steps in recycling cofilin and actin monomers.

Indexed as

Protein Structure, TertiaryActin Depolymerizing FactorsActinsAdaptor Proteins, Signal TransducingAdenosine DiphosphateAmino Acid SequenceAnimalsBinding SitesCell Cycle ProteinsCytoskeletal ProteinsModels, MolecularMolecular Sequence DataMultiprotein ComplexesProtein BindingSaccharomyces cerevisiae ProteinsSequence AlignmentActin Depolymerizing FactorsActinsAdaptor Proteins, Signal TransducingAdenosine DiphosphateADP-G-actinCell Cycle ProteinsCytoskeletal ProteinsMultiprotein ComplexesSaccharomyces cerevisiae ProteinsSRV2 protein, S cerevisiae

Identifiers

PMID19201756
PMCPMC2667778

What OpenQuestion holds

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Registered trials

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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.