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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2011
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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. |
format | Online Article Text |
id | pubmed-3164462 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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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