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Deciphering the rules governing assembly order of mammalian septin complexes

Septins are conserved GTP-binding proteins that assemble into lateral diffusion barriers and molecular scaffolds. Vertebrate genomes contain 9–17 septin genes that encode both ubiquitous and tissue-specific septins. Expressed septins may assemble in various combinations through both heterotypic and...

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Autores principales: Sellin, Mikael E., Sandblad, Linda, Stenmark, Sonja, Gullberg, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3164462/
https://www.ncbi.nlm.nih.gov/pubmed/21737677
http://dx.doi.org/10.1091/mbc.E11-03-0253
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author Sellin, Mikael E.
Sandblad, Linda
Stenmark, Sonja
Gullberg, Martin
author_facet Sellin, Mikael E.
Sandblad, Linda
Stenmark, Sonja
Gullberg, Martin
author_sort Sellin, Mikael E.
collection PubMed
description Septins are conserved GTP-binding proteins that assemble into lateral diffusion barriers and molecular scaffolds. Vertebrate genomes contain 9–17 septin genes that encode both ubiquitous and tissue-specific septins. Expressed septins may assemble in various combinations through both heterotypic and homotypic G-domain interactions. However, little is known regarding assembly states of mammalian septins and mechanisms directing ordered assembly of individual septins into heteromeric units, which is the focus of this study. Our analysis of the septin system in cells lacking or overexpressing selected septins reveals interdependencies coinciding with previously described homology subgroups. Hydrodynamic and single-particle data show that individual septins exist solely in the context of stable six- to eight-subunit core heteromers, all of which contain SEPT2 and SEPT6 subgroup members and SEPT7, while heteromers comprising more than six subunits also contain SEPT9. The combined data suggest a generic model for how the temporal order of septin assembly is homology subgroup-directed, which in turn determines the subunit arrangement of native heteromers. Because mammalian cells normally express multiple members and/or isoforms of some septin subgroups, our data also suggest that only a minor fraction of native heteromers are arranged as perfect palindromes.
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spelling pubmed-31644622011-11-16 Deciphering the rules governing assembly order of mammalian septin complexes Sellin, Mikael E. Sandblad, Linda Stenmark, Sonja Gullberg, Martin Mol Biol Cell Articles Septins are conserved GTP-binding proteins that assemble into lateral diffusion barriers and molecular scaffolds. Vertebrate genomes contain 9–17 septin genes that encode both ubiquitous and tissue-specific septins. Expressed septins may assemble in various combinations through both heterotypic and homotypic G-domain interactions. However, little is known regarding assembly states of mammalian septins and mechanisms directing ordered assembly of individual septins into heteromeric units, which is the focus of this study. Our analysis of the septin system in cells lacking or overexpressing selected septins reveals interdependencies coinciding with previously described homology subgroups. Hydrodynamic and single-particle data show that individual septins exist solely in the context of stable six- to eight-subunit core heteromers, all of which contain SEPT2 and SEPT6 subgroup members and SEPT7, while heteromers comprising more than six subunits also contain SEPT9. The combined data suggest a generic model for how the temporal order of septin assembly is homology subgroup-directed, which in turn determines the subunit arrangement of native heteromers. Because mammalian cells normally express multiple members and/or isoforms of some septin subgroups, our data also suggest that only a minor fraction of native heteromers are arranged as perfect palindromes. The American Society for Cell Biology 2011-09-01 /pmc/articles/PMC3164462/ /pubmed/21737677 http://dx.doi.org/10.1091/mbc.E11-03-0253 Text en © 2011 Sellin et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Sellin, Mikael E.
Sandblad, Linda
Stenmark, Sonja
Gullberg, Martin
Deciphering the rules governing assembly order of mammalian septin complexes
title Deciphering the rules governing assembly order of mammalian septin complexes
title_full Deciphering the rules governing assembly order of mammalian septin complexes
title_fullStr Deciphering the rules governing assembly order of mammalian septin complexes
title_full_unstemmed Deciphering the rules governing assembly order of mammalian septin complexes
title_short Deciphering the rules governing assembly order of mammalian septin complexes
title_sort deciphering the rules governing assembly order of mammalian septin complexes
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3164462/
https://www.ncbi.nlm.nih.gov/pubmed/21737677
http://dx.doi.org/10.1091/mbc.E11-03-0253
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