Cargando…
Plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division
Cell cycle is one of the most fundamentally conserved biological processes of plants and mammals. Casein kinase1s (CK1s) are critical for cell proliferation in mammalian cells; however, how CK1s coordinate cell division in plants remains unknown. Through genetic and biochemical studies, here we demo...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8491028/ https://www.ncbi.nlm.nih.gov/pubmed/34608955 http://dx.doi.org/10.1093/plphys/kiab284 |
_version_ | 1784578667438931968 |
---|---|
author | Qu, Li Wei, Zhuang Chen, Hu-Hui Liu, Tao Liao, Kan Xue, Hong-Wei |
author_facet | Qu, Li Wei, Zhuang Chen, Hu-Hui Liu, Tao Liao, Kan Xue, Hong-Wei |
author_sort | Qu, Li |
collection | PubMed |
description | Cell cycle is one of the most fundamentally conserved biological processes of plants and mammals. Casein kinase1s (CK1s) are critical for cell proliferation in mammalian cells; however, how CK1s coordinate cell division in plants remains unknown. Through genetic and biochemical studies, here we demonstrated that plant CK1, Arabidopsis (Arabidopsis thaliana) EL1-like (AELs), regulate cell cycle/division by modulating the stability and inhibitory effects of Kip-related protein6 (KRP6) through phosphorylation. Cytological analysis showed that AELs deficiency results in suppressed cell-cycle progression mainly due to the decreased DNA replication rate at S phase and increased period of G2 phase. AELs interact with and phosphorylate KRP6 at serines 75 and 109 to stimulate KRP6’s interaction with E3 ligases, thus facilitating the KRP6 degradation through the proteasome. These results demonstrate the crucial roles of CK1s/AELs in regulating cell division through modulating cell-cycle rates and elucidate how CK1s/AELs regulate cell division by destabilizing the stability of cyclin-dependent kinase inhibitor KRP6 through phosphorylation, providing insights into the plant cell-cycle regulation through CK1s-mediated posttranslational modification. |
format | Online Article Text |
id | pubmed-8491028 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-84910282021-10-06 Plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division Qu, Li Wei, Zhuang Chen, Hu-Hui Liu, Tao Liao, Kan Xue, Hong-Wei Plant Physiol Regular Issue Cell cycle is one of the most fundamentally conserved biological processes of plants and mammals. Casein kinase1s (CK1s) are critical for cell proliferation in mammalian cells; however, how CK1s coordinate cell division in plants remains unknown. Through genetic and biochemical studies, here we demonstrated that plant CK1, Arabidopsis (Arabidopsis thaliana) EL1-like (AELs), regulate cell cycle/division by modulating the stability and inhibitory effects of Kip-related protein6 (KRP6) through phosphorylation. Cytological analysis showed that AELs deficiency results in suppressed cell-cycle progression mainly due to the decreased DNA replication rate at S phase and increased period of G2 phase. AELs interact with and phosphorylate KRP6 at serines 75 and 109 to stimulate KRP6’s interaction with E3 ligases, thus facilitating the KRP6 degradation through the proteasome. These results demonstrate the crucial roles of CK1s/AELs in regulating cell division through modulating cell-cycle rates and elucidate how CK1s/AELs regulate cell division by destabilizing the stability of cyclin-dependent kinase inhibitor KRP6 through phosphorylation, providing insights into the plant cell-cycle regulation through CK1s-mediated posttranslational modification. Oxford University Press 2021-06-19 /pmc/articles/PMC8491028/ /pubmed/34608955 http://dx.doi.org/10.1093/plphys/kiab284 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of American Society of Plant Biologists. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (https://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Regular Issue Qu, Li Wei, Zhuang Chen, Hu-Hui Liu, Tao Liao, Kan Xue, Hong-Wei Plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division |
title | Plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division |
title_full | Plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division |
title_fullStr | Plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division |
title_full_unstemmed | Plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division |
title_short | Plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division |
title_sort | plant casein kinases phosphorylate and destabilize a cyclin-dependent kinase inhibitor to promote cell division |
topic | Regular Issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8491028/ https://www.ncbi.nlm.nih.gov/pubmed/34608955 http://dx.doi.org/10.1093/plphys/kiab284 |
work_keys_str_mv | AT quli plantcaseinkinasesphosphorylateanddestabilizeacyclindependentkinaseinhibitortopromotecelldivision AT weizhuang plantcaseinkinasesphosphorylateanddestabilizeacyclindependentkinaseinhibitortopromotecelldivision AT chenhuhui plantcaseinkinasesphosphorylateanddestabilizeacyclindependentkinaseinhibitortopromotecelldivision AT liutao plantcaseinkinasesphosphorylateanddestabilizeacyclindependentkinaseinhibitortopromotecelldivision AT liaokan plantcaseinkinasesphosphorylateanddestabilizeacyclindependentkinaseinhibitortopromotecelldivision AT xuehongwei plantcaseinkinasesphosphorylateanddestabilizeacyclindependentkinaseinhibitortopromotecelldivision |