Publication:
MAPK‑dependent control of mitotic progression in S. pombe

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dc.contributor.authorIglesias Romero, Ana Belén
dc.contributor.authorSoto Pino, Teresa
dc.contributor.authorFlor Parra, Ignacio
dc.contributor.authorSalas Pino, Silvia
dc.contributor.authorRuiz Romero, Gabriel
dc.contributor.authorGould, Kathleen L.
dc.contributor.authorCansado Vizoso, José
dc.contributor.authorDaga, Rafael R.
dc.contributor.departmentGenética y Microbiología
dc.contributor.otherFacultades de la UMU::Facultad de Biología
dc.date.accessioned2026-01-19T12:05:45Z
dc.date.available2026-01-19T12:05:45Z
dc.date.copyright© The Authors 2024.
dc.date.issued2024-03-25
dc.description.abstractBackground: Mitogen-activated protein kinases (MAPKs) preserve cell homeostasis by transducing physicochemical fluctuations of the environment into multiple adaptive responses. These responses involve transcriptional rewiring and the regulation of cell cycle transitions, among others. However, how stress conditions impinge mitotic progression is largely unknown. The mitotic checkpoint is a surveillance mechanism that inhibits mitotic exit in situations of defective chromosome capture, thus preventing the generation of aneuploidies. In this study, we investigate the role of MAPK Pmk1 in the regulation of mitotic exit upon stress. Results: We show that Schizosaccharomyces pombe cells lacking Pmk1, the MAP kinase effector of the cell integrity pathway (CIP), are hypersensitive to microtubule damage and defective in maintaining a metaphase arrest. Epistasis analysis suggests that Pmk1 is involved in maintaining spindle assembly checkpoint (SAC) signaling, and its deletion is additive to the lack of core SAC components such as Mad2 and Mad3. Strikingly, pmk1Δ cells show up to twofold increased levels of the anaphase-promoting complex (APC/C) activator Cdc20Slp1 during unperturbed growth. We demonstrate that Pmk1 physically interacts with Cdc20Slp1 N-terminus through a canonical MAPK docking site. Most important, the Cdc20Slp1 pool is rapidly degraded in stressed cells undergoing mitosis through a mechanism that requires MAPK activity, Mad3, and the proteasome, thus resulting in a delayed mitotic exit. Conclusions: Our data reveal a novel function of MAPK in preventing mitotic exit and activation of cytokinesis in response to stress. The regulation of Cdc20Slp1 turnover by MAPK Pmk1 provides a key mechanism by which the timing of mitotic exit can be adjusted relative to environmental conditions.
dc.formatapplication/pdf
dc.format.extent18
dc.identifier.citationBMC Biology, 2024, Vol. 22 : 71
dc.identifier.doihttps://doi.org/10.1186/s12915-024-01865-6
dc.identifier.eissn1741-7007
dc.identifier.urihttp://hdl.handle.net/10201/188071
dc.languageeng
dc.publisherBioMed Central
dc.relationThis work was supported by grants PID2021-128408OB-I00 and PGC2018-099849-B-I00 funded by MCIN/AEI/https://doi.org/10.13039/501100011033and “ERDF A way of making Europe” to R.R. Daga, grant PID2020-112569 GB-I00 funded by MCIN/AEI/https://doi.org/10.13039/501100011033 to J. Cansado, grants PY20_00807 to R.R. Dagaand UPO-1264663 to S. Salas-Pino funded by the UPO-FEDER-Conserjería de Economía, Conocimiento, Empresas y Universidad, Junta de Andalucía. PAIDI 2020, grant 20856/PI/18 funded by the Fundación Séneca de la Región de Murcia to J. Cansado and by National Institutes of Health R35GM131799 to K.L.Gould.
dc.relation.publisherversionhttps://link.springer.com/article/10.1186/s12915-024-01865-6
dc.rightsAttribution 4.0 International*
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectMAPK
dc.subjectCIP
dc.subjectSAPK
dc.subjectPmk1
dc.subjectSty1
dc.subjectSpindle assembly checkpoint
dc.subjectMCC
dc.subjectCDC20/Slp1
dc.subjectAPC/C
dc.subjectOsmotic stress
dc.subjectMitosis
dc.subjectCytokinesis
dc.subject.odsObjetivo 3: Salud
dc.titleMAPK‑dependent control of mitotic progression in S. pombe
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/publishedVersion
dspace.entity.typePublicationes
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relation.isAuthorOfPublicationadbf6152-5be5-40ed-82ad-558028639faf
relation.isAuthorOfPublication.latestForDiscoveryfce4a194-acc9-46a0-b74d-412344df138c
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