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YFR016c/Aip5 is part of an actin nucleation complex in yeast
The polarisome comprises a network of proteins that organizes polar growth in yeast and filamentous fungi. The yeast formin Bni1 and the actin nucleation-promoting factor Bud6 are subunits of the polarisome that together catalyze the formation of actin cables below the tip of yeast cells. We identif...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists Ltd
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6737964/ https://www.ncbi.nlm.nih.gov/pubmed/31362951 http://dx.doi.org/10.1242/bio.044024 |
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author | Glomb, Oliver Bareis, Lara Johnsson, Nils |
author_facet | Glomb, Oliver Bareis, Lara Johnsson, Nils |
author_sort | Glomb, Oliver |
collection | PubMed |
description | The polarisome comprises a network of proteins that organizes polar growth in yeast and filamentous fungi. The yeast formin Bni1 and the actin nucleation-promoting factor Bud6 are subunits of the polarisome that together catalyze the formation of actin cables below the tip of yeast cells. We identified YFR016c (Aip5) as an interaction partner of Bud6 and the polarisome scaffold Spa2. Yeast cells lacking Aip5 display a reduced number of actin cables. Aip5 binds with its N-terminal region to Spa2 and with its C-terminal region to Bud6. Both interactions collaborate to localize Aip5 at bud tip and neck, and are required to stimulate the formation of actin cables. Our experiments characterize Aip5 as a novel subunit of a complex that regulates the number of actin filaments at sites of polar growth. |
format | Online Article Text |
id | pubmed-6737964 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The Company of Biologists Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-67379642019-09-12 YFR016c/Aip5 is part of an actin nucleation complex in yeast Glomb, Oliver Bareis, Lara Johnsson, Nils Biol Open Research Article The polarisome comprises a network of proteins that organizes polar growth in yeast and filamentous fungi. The yeast formin Bni1 and the actin nucleation-promoting factor Bud6 are subunits of the polarisome that together catalyze the formation of actin cables below the tip of yeast cells. We identified YFR016c (Aip5) as an interaction partner of Bud6 and the polarisome scaffold Spa2. Yeast cells lacking Aip5 display a reduced number of actin cables. Aip5 binds with its N-terminal region to Spa2 and with its C-terminal region to Bud6. Both interactions collaborate to localize Aip5 at bud tip and neck, and are required to stimulate the formation of actin cables. Our experiments characterize Aip5 as a novel subunit of a complex that regulates the number of actin filaments at sites of polar growth. The Company of Biologists Ltd 2019-07-30 /pmc/articles/PMC6737964/ /pubmed/31362951 http://dx.doi.org/10.1242/bio.044024 Text en © 2019. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/4.0This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Research Article Glomb, Oliver Bareis, Lara Johnsson, Nils YFR016c/Aip5 is part of an actin nucleation complex in yeast |
title | YFR016c/Aip5 is part of an actin nucleation complex in yeast |
title_full | YFR016c/Aip5 is part of an actin nucleation complex in yeast |
title_fullStr | YFR016c/Aip5 is part of an actin nucleation complex in yeast |
title_full_unstemmed | YFR016c/Aip5 is part of an actin nucleation complex in yeast |
title_short | YFR016c/Aip5 is part of an actin nucleation complex in yeast |
title_sort | yfr016c/aip5 is part of an actin nucleation complex in yeast |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6737964/ https://www.ncbi.nlm.nih.gov/pubmed/31362951 http://dx.doi.org/10.1242/bio.044024 |
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