Evidence map›Paper›PMID 22918953›Full record

ArticleMolecular biology of the cell2012

Regulation of the formin Bnr1 by septins anda MARK/Par1-family septin-associated kinase.

Shawnna M Buttery, Keiko Kono, Ema Stokasimov, David Pellman

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Length control emerges from cytoskeletal network geometry.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Length control emerges from cytoskeletal network geometry.bioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Genetically inspired in vitro reconstitution ofMolecular biology of the cell · 2020
    Article
  15. Article
  16. Mechanics and regulation of cytokinesis in budding yeast.Seminars in cell & developmental biology · 2017
    Review
  17. Article
  18. Article
  19. 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

4 authors.

Shawnna M ButteryHoward Hughes Medical Institute, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.
Keiko Kono
Ema Stokasimov
David Pellman

Funding

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
Regulation and Mechanism of Bni1 Activity In VivoF32GM076895 · NIGMS · DANA-FARBER CANCER INST · PI BUTTERY, SHAWNNA MARIE · 2006 to 2007
$99k
NIGMS NIH HHS F32 GM076895NIGMS NIH HHS GM61345NIGMS NIH HHS R01 GM061345NIGMS NIH HHS R37 GM061345
6 · The paper itself

Abstract

Formin-family proteins promote the assembly of linear actin filaments and are required to generate cellular actin structures, such as actin stress fibers and the cytokinetic actomyosin contractile ring. Many formin proteins are regulated by an autoinhibition mechanism involving intramolecular binding of a Diaphanous inhibitory domain and a Diaphanous autoregulatory domain. However, the activation mechanism for these Diaphanous-related formins (DRFs) is not completely understood. Although small GTPases play an important role in relieving autoinhibition, other factors likely contribute. Here we describe a requirement for the septin Shs1 and the septin-associated kinase Gin4 for the localization and in vivo activity of the budding yeast DRF Bnr1. In budding yeast strains in which the other formin, Bni1, is conditionally inactivated, the loss of Gin4 or Shs1 results in the loss of actin cables and cell death, similar to the loss of Bnr1. The defects in these strains can be suppressed by constitutive activation of Bnr1. Gin4 is involved in both the localization and activation of Bnr1, whereas the septin Shs1 is required for Bnr1 activation but not its localization. Gin4 promotes the activity of Bnr1 independently of the Gin4 kinase activity, and Gin4 lacking its kinase domain binds to the critical localization region of Bnr1. These data reveal novel regulatory links between the actin and septin cytoskeletons.

Indexed as

Multigene FamilyActinsCell PolarityCyclin-Dependent KinasesCytoskeletal ProteinsEnzyme ActivationMutationProtein BindingProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsStructure-Activity RelationshipActinsBNR1 protein, S cerevisiaeCyclin-Dependent KinasesCytoskeletal ProteinsGIN4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSeptins

Identifiers

PMID22918953
PMCPMC3469519

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.