Evidence map›Paper›PMID 27806918›Full record

ArticleJournal of molecular biology2016

Effects of Bni5 Binding on Septin Filament Organization.

Elizabeth A Booth, Sarah M Sterling, Dustin Dovala, Eva Nogales, Jeremy Thorner

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.2field-weighted citation impact, top 34% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  4. Article
  5. Review
  6. Article
  7. 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

5 authors at 3 institutions in 1 country.

Elizabeth A BoothDivision of Biochemistry, Biophysics, and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA. Electronic address: elizabeth.booth@Grifols.com.
Sarah M SterlingDivision of Biochemistry, Biophysics, and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA. Electronic address: smsterling@berkeley.edu.
Dustin DovalaProgram in Microbial Pathogenesis and Host Defense, Department of Microbiology and Immunology, University of California School of Medicine, San Francisco, CA 94143, USA. Electronic address: dustin.dovala@novartis.com.
Eva NogalesDivision of Biochemistry, Biophysics, and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA; Life Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA. Electronic address: ENogales@lbl.gov.
Jeremy ThornerDivision of Biochemistry, Biophysics, and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA. Electronic address: jthorner@berkeley.edu.
University of California, Berkeley · USLawrence Berkeley National Laboratory · 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
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM021841NIGMS NIH HHS R01 GM101314
6 · The paper itself

Abstract

Septins are a protein family found in all eukaryotes (except higher plants) that have roles in membrane remodeling and formation of diffusion barriers and as a scaffold to recruit other proteins. In budding yeast, proper execution of cytokinesis and cell division requires the formation of a collar of circumferential filaments at the bud neck. These filaments are assembled from apolar septin hetero-octamers. Currently, little is known about the mechanisms that control the arrangement and dynamics of septin structures. In this study, we utilized both Förster resonance energy transfer and electron microscopy to analyze the biophysical properties of the septin-binding protein Bni5 and how its association with septin filaments affects their organization. We found that the interaction of Bni5 with the terminal subunit (Cdc11) at the junctions between adjacent hetero-octamers in paired filaments is highly cooperative. Both the C-terminal end of Bni5 and the C-terminal extension of Cdc11 make important contributions to their interaction. Moreover, this binding may stabilize the dimerization of Bni5, which, in turn, forms cross-filament braces that significantly narrow, and impose much more uniform spacing on, the gap between paired filaments.

Indexed as

Protein MultimerizationFluorescence Resonance Energy TransferMicroscopy, ElectronModels, BiologicalModels, ChemicalModels, MolecularProtein BindingProtein Interaction MappingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsBNI5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsanalytical ultracentrifugationelectron microscopyfield-flow fractionationFRET analysisyeast (Saccharomyces cerevisiae)

Identifiers

PMID27806918
PMCPMC5138130
OpenAlexW2541655129

What Socratic 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 Socratic graph.