Evidence map›Paper›PMID 33263440›Full record

ArticleMolecular biology of the cell2021

Revised subunit order of mammalian septin complexes explains their in vitro polymerization properties.

Forooz Soroor, Moshe S Kim, Oliva Palander, Yadu Balachandran, Richard F Collins, Samir Benlekbir, John L Rubinstein, William S Trimble

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.4field-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

48 citing papers in PubMed, 82 citations in OpenAlex.

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  15. Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024
    Article
  16. Two Septin Complexes Mediate Actin Dynamics During Cell Wound Repair.bioRxiv : the preprint server for biology · 2023
    Article
  17. Article
  18. Reduced Expression of Septin7 Hinders Skeletal Muscle Regeneration.International journal of molecular sciences · 2023
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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

8 authors at 2 institutions in 1 country.

Forooz SoroorCell Biology Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Moshe S KimCell Biology Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Oliva PalanderCell Biology Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Yadu BalachandranCell Biology Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Richard F CollinsCell Biology Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Samir BenlekbirMolecular Medicine Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
John L RubinsteinMolecular Medicine Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
William S TrimbleCell Biology Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

CIHR PJT-162194
6 · The paper itself

Abstract

Septins are conserved GTP-binding cytoskeletal proteins that polymerize into filaments by end-to-end joining of hetero-oligomeric complexes. In human cells, both hexamers and octamers exist, and crystallography studies predicted the order of the hexamers to be SEPT7-SEPT6-SEPT2-SEPT2-SEPT6-SEPT7, while octamers are thought to have the same core, but with SEPT9 at the ends. However, based on this septin organization, octamers and hexamers would not be expected to copolymerize due to incompatible ends. Here we isolated hexamers and octamers of specific composition from human cells and show that hexamers and octamers polymerize individually and, surprisingly, with each other. Binding of the Borg homology domain 3 (BD3) domain of Borg3 results in distinctive clustering of each filament type. Moreover, we show that the organization of hexameric and octameric complexes is inverted compared with its original prediction. This revised septin organization is congruent with the organization and behavior of yeast septins suggesting that their properties are more conserved than was previously thought.

Indexed as

AnimalsCell Cycle ProteinsCytoskeletonHeLa CellsHumansMammalsPolymerizationSeptinsCell Cycle ProteinsSeptins

Identifiers

PMID33263440
PMCPMC8098831
OpenAlexW3110240858

What Socratic 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 Socratic graph.