Evidence map›Paper›PMID 14657240›Full record

ArticleMolecular biology of the cell2004

A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin.

James B Moseley, Isabelle Sagot, Amity L Manning, Yingwu Xu, Michael J Eck, David Pellman, Bruce L Goode

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing 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

154 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Parallel actin monomers in the 8S complex of actin-INF2.Journal of biomolecular structure & dynamics · 2023
    Article
  14. FHODs: Nuclear tethered formins for nuclear mechanotransduction.Frontiers in cell and developmental biology · 2023
    Review
  15. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  16. Article
  17. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
  18. Article
  19. Article
  20. Article

94 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

7 authors.

James B MoseleyDepartment of Biology and The Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02454, USA.
Isabelle Sagot
Amity L Manning
Yingwu Xu
Michael J Eck
David Pellman
Bruce L Goode

Funding

MECHNISMS REGULATING ACTIN ASSEMBLYR01GM063691 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2002 to 2019
$7.5M
Inhibitor-sensitive and -resistant EGFR mutants from lung cancer and glioblastomaR01CA116020 · NCI · DANA-FARBER CANCER INST · PI ECK, MICHAEL J, MEYERSON, MATTHEW L. · 2006 to 2022
$5.1M
CELL POLARITY AND SPINDLE POSITIONR01GM061345 · NIGMS · DANA-FARBER CANCER INSTITUTE · PI PELLMAN, DAVID S · 2000 to 2011
$3.6M
Cell Cycle Control of the CytoskeletonR37GM061345 · NIGMS · DANA-FARBER CANCER INST · PI PELLMAN, DAVID S · 2014 to 2023
$3.4M
NCI NIH HHS R01 CA116020NIGMS NIH HHS GM61345NIGMS NIH HHS GM63691NIGMS NIH HHS R01 GM061345NIGMS NIH HHS R01 GM063691NIGMS NIH HHS R37 GM061345
6 · The paper itself

Abstract

Formins have conserved roles in cell polarity and cytokinesis and directly nucleate actin filament assembly through their FH2 domain. Here, we define the active region of the yeast formin Bni1 FH2 domain and show that it dimerizes. Mutations that disrupt dimerization abolish actin assembly activity, suggesting that dimers are the active state of FH2 domains. The Bni1 FH2 domain protects growing barbed ends of actin filaments from vast excesses of capping protein, suggesting that the dimer maintains a persistent association during elongation. This is not a species-specific mechanism, as the activities of purified mammalian formin mDia1 are identical to those of Bni1. Further, mDia1 partially complements BNI1 function in vivo, and expression of a dominant active mDia1 construct in yeast causes similar phenotypes to dominant active Bni1 constructs. In addition, we purified the Bni1-interacting half of the cell polarity factor Bud6 and found that it binds specifically to actin monomers and, like profilin, promotes rapid nucleotide exchange on actin. Bud6 and profilin show additive stimulatory effects on Bni1 activity and have a synthetic lethal genetic interaction in vivo. From these results, we propose a model in which Bni1 FH2 dimers nucleate and processively cap the elongating barbed end of the actin filament, and Bud6 and profilin generate a local flux of ATP-actin monomers to promote actin assembly.

Indexed as

Actin CytoskeletonAdenosine TriphosphateCell Cycle ProteinsCell PolarityCytoskeletonDimerizationMicrofilament ProteinsModels, MolecularProfilinsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateBni1 protein, S cerevisiaeBUD6 protein, S cerevisiaeCDC3 protein, S cerevisiaeCell Cycle ProteinsMicrofilament ProteinsProfilinsSaccharomyces cerevisiae Proteins

Identifiers

PMID14657240
PMCPMC329402

What OpenQuestion holds

Textmetadata
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.