Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4

Upon environmental changes, proliferating cells delay cell cycle to prevent further damage accumulation. Yeast Cip1 is a Cdk1 and Cln2-associated protein. However, the function and regulation of Cip1 are still poorly understood. Here we report that Cip1 expression is co-regulated by the cell-cycle-m...

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Autores: Chang, Ya-Lan, Tseng, Shun-Fu, Huang, Yu-Ching, Shen, Zih-Jie, Hsu, Pang-Hung, Hsieh, Meng-Hsun, Yang, Chia-Wei, Tognetti, Silvia, Canal de Torres, Berta, 1988-, Subirana, Laia, Wang, Chien-Wei, Chen, Hsiao-Tan, Lin, Chi-Ying, Posas Garriga, Francesc, Teng, Shu-Chun
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2017
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10230/33695
Acceso en línea:http://hdl.handle.net/10230/33695
http://dx.doi.org/10.1038/s41467-017-00080-y
Access Level:acceso abierto
Palabra clave:Checkpoints
Phosphorylation
Saccharomyces cerevisiae
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spelling Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4Chang, Ya-LanTseng, Shun-FuHuang, Yu-ChingShen, Zih-JieHsu, Pang-HungHsieh, Meng-HsunYang, Chia-WeiTognetti, SilviaCanal de Torres, Berta, 1988-Subirana, LaiaWang, Chien-WeiChen, Hsiao-TanLin, Chi-YingPosas Garriga, FrancescTeng, Shu-ChunCheckpointsPhosphorylationSaccharomyces cerevisiaeUpon environmental changes, proliferating cells delay cell cycle to prevent further damage accumulation. Yeast Cip1 is a Cdk1 and Cln2-associated protein. However, the function and regulation of Cip1 are still poorly understood. Here we report that Cip1 expression is co-regulated by the cell-cycle-mediated factor Mcm1 and the stress-mediated factors Msn2/4. Overexpression of Cip1 arrests cell cycle through inhibition of Cdk1-G1 cyclin complexes at G1 stage and the stress-activated protein kinase-dependent Cip1 T65, T69, and T73 phosphorylation may strengthen the Cip1and Cdk1-G1 cyclin interaction. Cip1 accumulation mainly targets Cdk1-Cln3 complex to prevent Whi5 phosphorylation and inhibit early G1 progression. Under osmotic stress, Cip1 expression triggers transient G1 delay which plays a functionally redundant role with another hyperosmolar activated CKI, Sic1. These findings indicate that Cip1 functions similarly to mammalian p21 as a stress-induced CDK inhibitor to decelerate cell cycle through G1 cyclins to cope with environmental stresses.A G1 cell cycle regulatory kinase Cip1 has been identified in budding yeast but how this is regulated is unclear. Here the authors identify cell cycle (Mcm1) and stress-mediated (Msn 2/4) transcription factors as regulating Cip1, causing stress induced CDK inhibition and delay in cell cycle progression.Nature Publishing Group201820182017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/33695http://dx.doi.org/10.1038/s41467-017-00080-yreponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésNature Communications. 2017 Jul 4;8(1):56info:eu-repo/grantAgreement/ES/1PE/BFU2015-64437-P© Nature Publishing Group. http://dx.doi.org/10.1038/s41467-017-00080-y. Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/http://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:recercat.cat:10230/336952026-05-29T05:05:01Z
dc.title.none.fl_str_mv Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4
title Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4
spellingShingle Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4
Chang, Ya-Lan
Checkpoints
Phosphorylation
Saccharomyces cerevisiae
title_short Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4
title_full Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4
title_fullStr Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4
title_full_unstemmed Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4
title_sort Yeast Cip1 is activated by environmental stress to inhibit Cdk1–G1 cyclins via Mcm1 and Msn2/4
dc.creator.none.fl_str_mv Chang, Ya-Lan
Tseng, Shun-Fu
Huang, Yu-Ching
Shen, Zih-Jie
Hsu, Pang-Hung
Hsieh, Meng-Hsun
Yang, Chia-Wei
Tognetti, Silvia
Canal de Torres, Berta, 1988-
Subirana, Laia
Wang, Chien-Wei
Chen, Hsiao-Tan
Lin, Chi-Ying
Posas Garriga, Francesc
Teng, Shu-Chun
author Chang, Ya-Lan
author_facet Chang, Ya-Lan
Tseng, Shun-Fu
Huang, Yu-Ching
Shen, Zih-Jie
Hsu, Pang-Hung
Hsieh, Meng-Hsun
Yang, Chia-Wei
Tognetti, Silvia
Canal de Torres, Berta, 1988-
Subirana, Laia
Wang, Chien-Wei
Chen, Hsiao-Tan
Lin, Chi-Ying
Posas Garriga, Francesc
Teng, Shu-Chun
author_role author
author2 Tseng, Shun-Fu
Huang, Yu-Ching
Shen, Zih-Jie
Hsu, Pang-Hung
Hsieh, Meng-Hsun
Yang, Chia-Wei
Tognetti, Silvia
Canal de Torres, Berta, 1988-
Subirana, Laia
Wang, Chien-Wei
Chen, Hsiao-Tan
Lin, Chi-Ying
Posas Garriga, Francesc
Teng, Shu-Chun
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Checkpoints
Phosphorylation
Saccharomyces cerevisiae
topic Checkpoints
Phosphorylation
Saccharomyces cerevisiae
description Upon environmental changes, proliferating cells delay cell cycle to prevent further damage accumulation. Yeast Cip1 is a Cdk1 and Cln2-associated protein. However, the function and regulation of Cip1 are still poorly understood. Here we report that Cip1 expression is co-regulated by the cell-cycle-mediated factor Mcm1 and the stress-mediated factors Msn2/4. Overexpression of Cip1 arrests cell cycle through inhibition of Cdk1-G1 cyclin complexes at G1 stage and the stress-activated protein kinase-dependent Cip1 T65, T69, and T73 phosphorylation may strengthen the Cip1and Cdk1-G1 cyclin interaction. Cip1 accumulation mainly targets Cdk1-Cln3 complex to prevent Whi5 phosphorylation and inhibit early G1 progression. Under osmotic stress, Cip1 expression triggers transient G1 delay which plays a functionally redundant role with another hyperosmolar activated CKI, Sic1. These findings indicate that Cip1 functions similarly to mammalian p21 as a stress-induced CDK inhibitor to decelerate cell cycle through G1 cyclins to cope with environmental stresses.A G1 cell cycle regulatory kinase Cip1 has been identified in budding yeast but how this is regulated is unclear. Here the authors identify cell cycle (Mcm1) and stress-mediated (Msn 2/4) transcription factors as regulating Cip1, causing stress induced CDK inhibition and delay in cell cycle progression.
publishDate 2017
dc.date.none.fl_str_mv 2017
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10230/33695
http://dx.doi.org/10.1038/s41467-017-00080-y
url http://hdl.handle.net/10230/33695
http://dx.doi.org/10.1038/s41467-017-00080-y
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Nature Communications. 2017 Jul 4;8(1):56
info:eu-repo/grantAgreement/ES/1PE/BFU2015-64437-P
dc.rights.none.fl_str_mv http://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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