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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...

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Detalles Bibliográficos
Autores principales: Glomb, Oliver, Bareis, Lara, Johnsson, Nils
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Company of Biologists Ltd 2019
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.
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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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