BIROT, Adrien; EGUIENTA, Karen; VAZQUEZ, Stephanie; CLAVEROL, Stephane; BONNEU, Marc; EKWALL, Karl; JAVERZAT, Jean-Paul; VAUR, Sabine

doi:10.15252/embj.201696050

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BIROT, Adrien
Institut de biochimie et génétique cellulaires [IBGC]

EGUIENTA, Karen
Institut de biochimie et génétique cellulaires [IBGC]

VAZQUEZ, Stephanie
Institut de biochimie et génétique cellulaires [IBGC]

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Embo Journal. 2017-05-15, vol. 36, n° 10, p. 1364-1378

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Cohesin 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.< Réduire

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

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