Evidence map›Paper›PMID 22767579›Full record

ArticleMolecular biology of the cell2012

Septin ring size scaling and dynamics require the coiled-coil region of Shs1p.

Rebecca A Meseroll, Louisa Howard, Amy S Gladfelter

Open access · greenAbstract 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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Septins and Generation of Asymmetries in Fungal Cells.Annual review of microbiology · 2015
    Review
  15. Septin assemblies form by diffusion-driven annealing on membranes.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Article
  17. Article
  18. Article
  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

3 authors at 1 institution in 1 country.

Rebecca A MeserollDepartment of Biological Sciences, Dartmouth College, Hanover, NH 03755, USA.
Louisa Howard
Amy S Gladfelter
Dartmouth College · US

Funding

HOST-MICROBE INTERACTIONST32AI007519 · NIAID · DARTMOUTH COLLEGE · PI DEBORAH A HOGAN · 1997 to 2026
$5.9M
NIAID NIH HHS T32 AI007519
6 · The paper itself

Abstract

Septins are conserved GTP-binding proteins that assemble into heteromeric complexes that form filaments and higher-order structures in cells. What directs filament assembly, determines the size of higher-order septin structures, and governs septin dynamics is still not well understood. We previously identified two kinases essential for septin ring assembly in the filamentous fungus Ashbya gossypii and demonstrate here that the septin Shs1p is multiphosphorylated at the C-terminus of the protein near the predicted coiled-coil domain. Expression of the nonphosphorylatable allele shs1-9A does not mimic the loss of the kinase nor does complete truncation of the Shs1p C-terminus. Surprisingly, however, loss of the C-terminus or the predicted coiled-coil domain of Shs1p generates expanded zones of septin assemblies and ectopic septin fibers, as well as aberrant cell morphology. The expanded structures form coincident with ring assembly and are heteromeric. Interestingly, while septin recruitment to convex membranes is increased, septin localization is diminished at concave membranes in these mutants. Additionally, the loss of the coiled-coil leads to increased mobility of Shs1p. These data indicate the coiled-coil of Shs1p is an important negative regulator of septin ring size and mobility, and its absence may make septin assembly sensitive to local membrane curvature.

Indexed as

Cell Cycle ProteinsCytoskeletal ProteinsFungal ProteinsGTP-Binding ProteinsProtein Structure, TertiarySaccharomyces cerevisiae ProteinsSaccharomycetalesSeptinsCell Cycle ProteinsCytoskeletal ProteinsFungal ProteinsGTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSeptinsSHS1 protein, S cerevisiae

Identifiers

PMID22767579
PMCPMC3431940
OpenAlexW2111391224

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.