Evidence map›Paper›PMID 25971665›Full record

ArticleGenetics2015

Comprehensive Genetic Analysis of Paralogous Terminal Septin Subunits Shs1 and Cdc11 in Saccharomyces cerevisiae.

Gregory C Finnigan, Julie Takagi, Christina Cho, Jeremy Thorner

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

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  6. The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021
    Review
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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 at 3 institutions in 1 country.

Gregory C FinniganDivision of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202.
Julie TakagiDepartment of Microbiology and Immunology, University of California School of Medicine, San Francisco, California 94158-2200.
Christina ChoHarvard School of Dental Medicine, Boston, Massachusetts 02115.
Jeremy ThornerDivision of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202 Department of Microbiology and Immunology, University of California School of Medicine, San Francisco, California 94158-2200 Harvard School of Dental Medicine, Boston, Massachusetts 02115 jthorner@berkeley.edu.
University of California, Berkeley · USHarvard University · USUniversity of California, San Francisco · 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
YEAST PEPTIDE HORMONE SYNTHESIS AND SIGNAL TRANSDUCTIONR37GM021841 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 1989 to 1998
–
NIGMS NIH HHS GM101314NIGMS NIH HHS GM21841NIGMS NIH HHS R01 GM021841NIGMS NIH HHS R01 GM101314
6 · The paper itself

Abstract

Septins are a family of GTP-binding proteins considered to be cytoskeletal elements because they self-assemble into filaments and other higher-order structures in vivo. In budding yeast, septins establish a diffusion barrier at the bud neck between a mother and daughter cell, promote membrane curvature there, and serve as a scaffold to recruit other proteins to the site of cytokinesis. However, the mechanism by which any septin engages a partner protein has been unclear. The two most related and recently evolved subunits appear to be Cdc11 and Shs1, and the basic building blocks for assembling septin structures are hetero-octameric rods (Cdc11-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Cdc11 and Shs1-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Shs1). Loss of Cdc11 is not normally tolerated, whereas cells lacking Shs1 do not appear grossly abnormal. We established several different sensitized genetic backgrounds wherein Shs1 is indispensable, which allowed us to carry out the first comprehensive and detailed genetic analysis of Shs1 in vivo. Our analysis revealed several novel insights, including: (i) the sole portion of Shs1 essential for its function is a predicted coiled-coil-forming segment in its C-terminal extension (CTE); (ii) the CTE of Cdc11 shares this function; (iii) this role for the CTEs of Cdc11 and Shs1 is quite distinct from that of the CTEs of Cdc3 and Cdc12; and (iv) heterotypic Cdc11 and Shs1 junctions likely occur in vivo.

Indexed as

Amino Acid MotifsCell Cycle ProteinsCytokinesisCytoskeletal ProteinsCytoskeletonMutationProfilinsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCDC11 protein, S cerevisiaeCDC12 protein, S cerevisiaeCDC3 protein, S cerevisiaeCell Cycle ProteinsCytoskeletal ProteinsProfilinsSaccharomyces cerevisiae ProteinsSHS1 protein, S cerevisiaecomplexescytoskeletonfilamentsmutantsyeast

Identifiers

PMID25971665
PMCPMC4512546
OpenAlexW2117239697

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.