Evidence map›Paper›PMID 22144691›Full record

ArticleThe Journal of cell biology2011

Subunit-dependent modulation of septin assembly: budding yeast septin Shs1 promotes ring and gauze formation.

Galo Garcia, Aurelie Bertin, Zhu Li, Yi Song, Michael A McMurray, Jeremy Thorner, Eva Nogales

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

108 citing papers in PubMed, 185 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Localization and function of septins are susceptible to epitope tagging.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  14. Article
  15. The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

48 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 at 1 institution in 1 country.

Galo GarciaDivision of Biochemistry and Molecular Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Aurelie Bertin
Zhu Li
Yi Song
Michael A McMurray
Jeremy Thorner
Eva Nogales
University of California, Berkeley · 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 conserved guanosine triphosphate-binding cytoskeletal proteins involved in membrane remodeling. In budding yeast, five mitotic septins (Cdc3, Cdc10, Cdc11, Cdc12, and Shs1), which are essential for cytokinesis, transition during bud growth from a patch to a collar, which splits into two rings in cytokinesis and is disassembled before the next cell cycle. Cdc3, Cdc10, Cdc11, and Cdc12 form an apolar octameric rod with Cdc11 at each tip, which polymerizes into straight paired filaments. We show that Shs1 substitutes for Cdc11, resulting in octameric rods that do not polymerize into filaments but associate laterally, forming curved bundles that close into rings. In vivo, half of shs1Δ mutant cells exhibit incomplete collars and disrupted neck filaments. Importantly, different phosphomimetic mutations in Shs1 can either prevent ring formation or promote formation of a gauzelike meshwork. These results show that a single alternative terminal subunit is sufficient to confer a distinctive higher-order septin ultrastructure that can be further regulated by phosphorylation.

Indexed as

Cell Cycle ProteinsCytoskeletal ProteinsMutationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCDC11 protein, S cerevisiaeCell Cycle ProteinsCytoskeletal ProteinsSaccharomyces cerevisiae ProteinsSHS1 protein, S cerevisiae

Identifiers

PMID22144691
PMCPMC3241732
OpenAlexW2127422455

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.