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Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring
The contractile ring must anchor to the plasma membrane and cell wall to transmit its tension. F-BAR domain containing proteins including Imp2p and Cdc15p in fission yeast are likely candidate anchoring proteins based on their mutant phenotypes. Cdc15p is a node component, links the actin bundle to...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9727792/ https://www.ncbi.nlm.nih.gov/pubmed/36287824 http://dx.doi.org/10.1091/mbc.E22-06-0221 |
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author | Bellingham-Johnstun, Kimberly Commer, Blake Levesque, Brié Tyree, Zoe L. Laplante, Caroline |
author_facet | Bellingham-Johnstun, Kimberly Commer, Blake Levesque, Brié Tyree, Zoe L. Laplante, Caroline |
author_sort | Bellingham-Johnstun, Kimberly |
collection | PubMed |
description | The contractile ring must anchor to the plasma membrane and cell wall to transmit its tension. F-BAR domain containing proteins including Imp2p and Cdc15p in fission yeast are likely candidate anchoring proteins based on their mutant phenotypes. Cdc15p is a node component, links the actin bundle to the plasma membrane, recruits Bgs1p to the division plane, prevents contractile ring sliding, and contributes to the stiffness of the contractile ring. Less is known about Imp2p. We found that similarly to Cdc15p, Imp2p contributes to the stiffness of the contractile ring and assembles into protein clusters. Imp2p clusters contain approximately eight Imp2p dimers and depend on the actin network for their stability at the division plane. Importantly, Imp2p and Cdc15p reciprocally affect the amount of each other in the contractile ring, indicating that the two proteins influence each other during cytokinesis, which may partially explain their similar phenotypes. |
format | Online Article Text |
id | pubmed-9727792 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-97277922023-02-02 Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring Bellingham-Johnstun, Kimberly Commer, Blake Levesque, Brié Tyree, Zoe L. Laplante, Caroline Mol Biol Cell Articles The contractile ring must anchor to the plasma membrane and cell wall to transmit its tension. F-BAR domain containing proteins including Imp2p and Cdc15p in fission yeast are likely candidate anchoring proteins based on their mutant phenotypes. Cdc15p is a node component, links the actin bundle to the plasma membrane, recruits Bgs1p to the division plane, prevents contractile ring sliding, and contributes to the stiffness of the contractile ring. Less is known about Imp2p. We found that similarly to Cdc15p, Imp2p contributes to the stiffness of the contractile ring and assembles into protein clusters. Imp2p clusters contain approximately eight Imp2p dimers and depend on the actin network for their stability at the division plane. Importantly, Imp2p and Cdc15p reciprocally affect the amount of each other in the contractile ring, indicating that the two proteins influence each other during cytokinesis, which may partially explain their similar phenotypes. The American Society for Cell Biology 2022-11-18 /pmc/articles/PMC9727792/ /pubmed/36287824 http://dx.doi.org/10.1091/mbc.E22-06-0221 Text en © 2022 Bellingham-Johnstun, Commer, et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. https://creativecommons.org/licenses/by-nc-sa/4.0/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 4.0 International Creative Commons License. |
spellingShingle | Articles Bellingham-Johnstun, Kimberly Commer, Blake Levesque, Brié Tyree, Zoe L. Laplante, Caroline Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring |
title | Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring |
title_full | Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring |
title_fullStr | Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring |
title_full_unstemmed | Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring |
title_short | Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring |
title_sort | imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9727792/ https://www.ncbi.nlm.nih.gov/pubmed/36287824 http://dx.doi.org/10.1091/mbc.E22-06-0221 |
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