Evidence map›Paper›PMID 21497764›Full record

ArticleDevelopmental cell2011

Septin filament formation is essential in budding yeast.

Michael A McMurray, Aurelie Bertin, Galo Garcia, Lisa Lam, Eva Nogales, Jeremy Thorner

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

92 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
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  9. Article
  10. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Two Septin Complexes Mediate Actin Dynamics During Cell Wound Repair.bioRxiv : the preprint server for biology · 2023
    Article
  16. Article
  17. Chaperone requirements for de novo folding ofMolecular biology of the cell · 2022
    Article
  18. Article
  19. Article
  20. Article

32 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

6 authors at 2 institutions in 1 country.

Michael A McMurrayDivision of Biochemistry and Molecular Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Aurelie Bertin
Galo Garcia
Lisa Lam
Eva Nogales
Jeremy Thorner
University of California, Berkeley · USLawrence Berkeley National Laboratory · US

Funding

Yeast Protein Kinase Signaling Networks: Specificity, Regulation and FunctionR01GM021841 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 1985 to 2019
$11.8M
Septin Filaments: Architecture, Assembly and RegulationR01GM101314 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 2013 to 2020
$2.1M
Mechanisms of assembly and inheritance of yeast septin-containing structuresR00GM086603 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI MCMURRAY, MICHAEL A · 2011 to 2013
$711k
Mechanisms of assembly and inheritance of yeast septin-containing structuresK99GM086603 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MCMURRAY, MICHAEL A · 2009 to 2010
$180k
Howard Hughes Medical InstituteNIGMS NIH HHS K99 GM086603NIGMS NIH HHS K99 GM86603NIGMS NIH HHS R00 GM086603NIGMS NIH HHS R01 GM021841NIGMS NIH HHS R01 GM101314NIGMS NIH HHS R01 GM21841
6 · The paper itself

Abstract

Septins are GTP-binding proteins that form ordered, rod-like multimeric complexes and polymerize into filaments, but how such supramolecular structure is related to septin function was unclear. In Saccharomyces cerevisiae, four septins form an apolar hetero-octamer (Cdc11-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Cdc11) that associates end-to-end to form filaments. We show that septin filament assembly displays previously unanticipated plasticity. Cells lacking Cdc10 or Cdc11 are able to divide because the now-exposed subunits (Cdc3 or Cdc12, respectively) retain an ability to homodimerize via their so-called G interface, thereby allowing for filament assembly. In such cdc10Δ and cdc11Δ cells, the remaining septins, like wild-type complexes, localize to the cortex at the bud neck and compartmentalize nonseptin factors, consistent with a diffusion barrier composed of continuous filaments in intimate contact with the plasma membrane. Conversely, Cdc10 or Cdc11 mutants that cannot self-associate, but "cap" Cdc3 or Cdc12, respectively, prevent filament formation, block cortical localization, and kill cells.

Indexed as

Genes, EssentialRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSeptins

Identifiers

PMID21497764
PMCPMC3079881
OpenAlexW2037747220

What OpenQuestion holds

Textmetadata
LicenceTDM
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.