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RNA-Binding Protein Rnc1 Regulates Cell Length at Division and Acute Stress Response in Fission Yeast through Negative Feedback Modulation of the Stress-Activated Mitogen-Activated Protein Kinase Pathway

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dc.contributor.authorPrieto-Ruíz, Francisco
dc.contributor.authorVicente-Soler, Jero
dc.contributor.authorFranco Sánchez, Alejandro
dc.contributor.authorGómez-Gil, Elisa
dc.contributor.authorSánchez-Marinas, Marta
dc.contributor.authorVázquez-Marín, Beatriz
dc.contributor.authorAligué, Rosa
dc.contributor.authorMadrid, Marisa
dc.contributor.authorMoreno, Sergio
dc.contributor.authorSoto, Teresa
dc.contributor.authorCansado Vizoso, José
dc.contributor.departmentGenética y Microbiología
dc.date.accessioned2021-03-16T12:52:23Z
dc.date.available2021-03-16T12:52:23Z
dc.date.issued2020-02
dc.description.abstractRNA-binding proteins (RBPs) play a major role during control of mRNA localization, stability, and translation and are central to most cellular processes. In the fission yeast Schizosaccharomyces pombe, the multiple K homology (KH) domain RBP Rnc1 downregulates the activity of the cell integrity pathway (CIP) via stabilization of pmp1 mRNA, which encodes the Pmp1 phosphatase that inactivates Pmk1, the mitogen-activated protein kinase (MAPK) component of this signaling cascade. However, Rnc1 likely regulates the half-life/stability of additional mRNAs. We show that Rnc1 downregulates the activity of Sty1, the MAPK of the stress-activated MAPK pathway (SAPK), during control of cell length at division and recovery in response to acute stress. Importantly, this control strictly depends on Rnc1’s ability to bind mRNAs encoding activators (Wak1 MAPKKK, Wis1 MAPKK) and downregulators (Atf1 transcription factor, Pyp1 and Pyp2 phosphatases) of Sty1 phosphorylation throughits KH domains. Moreover, Sty1 is responsible for Rnc1 phosphorylation in vivo at multiple phosphosites during growth and stress, and these modifications trigger Rnc1 for proper binding and destabilization of the above mRNA targets. Phosphorylation by Sty1 prompts Rnc1-dependent mRNA destabilization to negatively control SAPK signaling, thus revealing an additional feedback mechanism that allows precise tuning of MAPK activity during unperturbed cell growth and stress.es
dc.formatapplication/pdfes
dc.format.extent54es
dc.identifier.citationmBio., 2020, vol 11 – nº 1, pp. e02815-19
dc.identifier.doi10.1128/mBio.02815-19
dc.identifier.urihttp://hdl.handle.net/10201/105006
dc.languageenges
dc.publisherAmerican Society for Microbiologyes
dc.relationÁmbito del proyecto (europeo, nacional o regional): Nacional Agencia/entidad financiadora: Ministerio de Economía, Industria y Competitividad (Ministerio de Ciencia, Innovacion y Universidades, Spain (grant reference BFU2017-82423-P to J.C.)) Convocatoria: 2017 Nombre del proyecto: Regulación por MAP quinasas del citoesqueleto de actina y la polaridad celular. Código: BFU2017-82423-Pes
dc.relation.publisherversionhttps://doi.org/10.1128/mBio.02815-19.2020es
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectMAP kinaseses
dc.subjectRNA-binding proteinses
dc.subjectfission yeastes
dc.subject.otherCDU::5 - Ciencias puras y naturales::57 - Biología::579 - Microbiologíaes
dc.titleRNA-Binding Protein Rnc1 Regulates Cell Length at Division and Acute Stress Response in Fission Yeast through Negative Feedback Modulation of the Stress-Activated Mitogen-Activated Protein Kinase Pathwayes
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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