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A second Wpl1 anti-cohesion pathway requires dephosphorylation of fission yeast kleisin Rad21 by PP4

hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorBIROT, Adrien
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorEGUIENTA, Karen
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorVAZQUEZ, Stephanie
hal.structure.identifierCentre de Génomique Fonctionnelle de Bordeaux [CGFB]
dc.contributor.authorCLAVEROL, Stephane
hal.structure.identifierCentre de Génomique Fonctionnelle de Bordeaux [CGFB]
dc.contributor.authorBONNEU, Marc
dc.contributor.authorEKWALL, Karl
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorJAVERZAT, Jean-Paul
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorVAUR, Sabine
dc.date.accessioned2020-07-09T14:17:12Z
dc.date.available2020-07-09T14:17:12Z
dc.date.issued2017-05-15
dc.identifier.issn0261-4189
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10357
dc.description.abstractEnCohesin mediates sister chromatid cohesion which is essential for chromosome segregation and repair. Sister chromatid cohesion requires an acetyl-transferase (Eso1 in fission yeast) counteracting Wpl1, promoting cohesin release from DNA. We report here that Wpl1 anti-cohesion function includes an additional mechanism. A genetic screen uncovered that Protein Phosphatase 4 (PP4) mutants allowed cell survival in the complete absence of Eso1. PP4 co-immunoprecipitated Wpl1 and cohesin and Wpl1 triggered Rad21 de-phosphorylation in a PP4-dependent manner. Relevant residues were identified and mapped within the central domain of Rad21. Phospho-mimicking alleles dampened Wpl1 anti-cohesion activity, while alanine mutants were neutral indicating that Rad21 phosphorylation would shelter cohesin from Wpl1 unless erased by PP4. Experiments in post-replicative cells lacking Eso1 revealed two cohesin populations. Type 1 was released from DNA by Wpl1 in a PP4-independent manner. Type 2 cohesin, however, remained DNA-bound and lost its cohesiveness in a manner depending on Wpl1-and PP4-mediated Rad21 de-phosphorylation. These results reveal that Wpl1 antagonizes sister chromatid cohesion by a novel pathway regulated by the phosphorylation status of the cohesin kleisin subunit.
dc.title.enA second Wpl1 anti-cohesion pathway requires dephosphorylation of fission yeast kleisin Rad21 by PP4
dc.typeArticle de revue
dc.identifier.doi10.15252/embj.201696050
dc.subject.halChimie/Matériaux
bordeaux.journalEmbo Journal
bordeaux.page1364-1378
bordeaux.volume36
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue10
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
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