Cargando…

Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast

Whereas actomyosin and septin ring organization and function in cytokinesis are thoroughly described, little is known regarding the mechanisms by which the actomyosin ring interacts with septins and associated proteins to coordinate cell division. Here we show that the protein product of YPL158C, Ai...

Descripción completa

Detalles Bibliográficos
Autores principales: Wolken, Dana M. Alessi, McInnes, Joseph, Pon, Liza A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3952846/
https://www.ncbi.nlm.nih.gov/pubmed/24451263
http://dx.doi.org/10.1091/mbc.E13-06-0317
_version_ 1782307270022922240
author Wolken, Dana M. Alessi
McInnes, Joseph
Pon, Liza A.
author_facet Wolken, Dana M. Alessi
McInnes, Joseph
Pon, Liza A.
author_sort Wolken, Dana M. Alessi
collection PubMed
description Whereas actomyosin and septin ring organization and function in cytokinesis are thoroughly described, little is known regarding the mechanisms by which the actomyosin ring interacts with septins and associated proteins to coordinate cell division. Here we show that the protein product of YPL158C, Aim44p, undergoes septin-dependent recruitment to the site of cell division. Aim44p colocalizes with Myo1p, the type II myosin of the contractile ring, throughout most of the cell cycle. The Aim44p ring does not contract when the actomyosin ring closes. Instead, it forms a double ring that associates with septin rings on mother and daughter cells after cell separation. Deletion of AIM44 results in defects in contractile ring closure. Aim44p coimmunoprecipitates with Hof1p, a conserved F-BAR protein that binds both septins and type II myosins and promotes contractile ring closure. Deletion of AIM44 results in a delay in Hof1p phosphorylation and altered Hof1p localization. Finally, overexpression of Dbf2p, a kinase that phosphorylates Hof1p and is required for relocalization of Hof1p from septin rings to the contractile ring and for Hof1p-triggered contractile ring closure, rescues the cytokinesis defect observed in aim44∆ cells. Our studies reveal a novel role for Aim44p in regulating contractile ring closure through effects on Hof1p.
format Online
Article
Text
id pubmed-3952846
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher The American Society for Cell Biology
record_format MEDLINE/PubMed
spelling pubmed-39528462014-05-30 Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast Wolken, Dana M. Alessi McInnes, Joseph Pon, Liza A. Mol Biol Cell Articles Whereas actomyosin and septin ring organization and function in cytokinesis are thoroughly described, little is known regarding the mechanisms by which the actomyosin ring interacts with septins and associated proteins to coordinate cell division. Here we show that the protein product of YPL158C, Aim44p, undergoes septin-dependent recruitment to the site of cell division. Aim44p colocalizes with Myo1p, the type II myosin of the contractile ring, throughout most of the cell cycle. The Aim44p ring does not contract when the actomyosin ring closes. Instead, it forms a double ring that associates with septin rings on mother and daughter cells after cell separation. Deletion of AIM44 results in defects in contractile ring closure. Aim44p coimmunoprecipitates with Hof1p, a conserved F-BAR protein that binds both septins and type II myosins and promotes contractile ring closure. Deletion of AIM44 results in a delay in Hof1p phosphorylation and altered Hof1p localization. Finally, overexpression of Dbf2p, a kinase that phosphorylates Hof1p and is required for relocalization of Hof1p from septin rings to the contractile ring and for Hof1p-triggered contractile ring closure, rescues the cytokinesis defect observed in aim44∆ cells. Our studies reveal a novel role for Aim44p in regulating contractile ring closure through effects on Hof1p. The American Society for Cell Biology 2014-03-15 /pmc/articles/PMC3952846/ /pubmed/24451263 http://dx.doi.org/10.1091/mbc.E13-06-0317 Text en © 2014 Wolken 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
Wolken, Dana M. Alessi
McInnes, Joseph
Pon, Liza A.
Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast
title Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast
title_full Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast
title_fullStr Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast
title_full_unstemmed Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast
title_short Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast
title_sort aim44p regulates phosphorylation of hof1p to promote contractile ring closure during cytokinesis in budding yeast
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3952846/
https://www.ncbi.nlm.nih.gov/pubmed/24451263
http://dx.doi.org/10.1091/mbc.E13-06-0317
work_keys_str_mv AT wolkendanamalessi aim44pregulatesphosphorylationofhof1ptopromotecontractileringclosureduringcytokinesisinbuddingyeast
AT mcinnesjoseph aim44pregulatesphosphorylationofhof1ptopromotecontractileringclosureduringcytokinesisinbuddingyeast
AT ponlizaa aim44pregulatesphosphorylationofhof1ptopromotecontractileringclosureduringcytokinesisinbuddingyeast