Revised subunit order of mammalian septin complexes explains their in vitro polymerization properties-Reference-Cited by-同舟云学术

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

Published:2021-02-01 Issue:3 Volume:32 Page:289-300
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Soroor Forooz¹²,Kim Moshe S.¹,Palander Oliva¹²,Balachandran Yadu¹,Collins Richard F.¹,Benlekbir Samir³,Rubinstein John L.³²,Trimble William S.¹²

Affiliation:

1. Cell Biology Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada

2. Department of Biochemistry, University of Toronto, Toronto, ON M5G 1A8, Canada

3. Molecular Medicine Program, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada

Abstract

Septins are filamentous GTPases that polymerize from hetero-oligomeric complexes. Their order was based on crystallographic studies, but we provide evidence that the canonical organization is inverted. This revised septin organization is congruent with the organization and behavior of yeast septins, suggesting that their properties are conserved.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference37 articles.

1. Septins at a glance

2. Saccharomyces cerevisiae septins: Supramolecular organization of heterooligomers and the mechanism of filament assembly

3. A Förster Resonance Energy Transfer (FRET)-based System Provides Insight into the Ordered Assembly of Yeast Septin Hetero-octamers

4. Phylogenetic and evolutionary analysis of the septin protein family in metazoan

5. Distinct roles of septins in cytokinesis: SEPT9 mediates midbody abscission

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