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000182432 041__ $$aEnglish
000182432 082__ $$a570
000182432 1001_ $$aRathi, Siddhi$$b0
000182432 245__ $$aThe budding yeast GSK-3 homologue Mck1 is an essential component of the spindle position checkpoint.
000182432 260__ $$aLondon$$bRoyal Society Publishing$$c2022
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000182432 520__ $$aThe spindle position checkpoint (SPOC) is a mitotic surveillance mechanism in Saccharomyces cerevisiae that prevents cells from completing mitosis in response to spindle misalignment, thereby contributing to genomic integrity. The kinase Kin4, one of the most downstream SPOC components, is essential to stop the mitotic exit network (MEN), a signalling pathway that promotes the exit from mitosis and cell division. Previous work, however, suggested that a Kin4-independent pathway contributes to SPOC, yet the underlying mechanisms remain elusive. Here, we established the glycogen-synthase-kinase-3 (GSK-3) homologue Mck1, as a novel component that works independently of Kin4 to engage SPOC. Our data indicate that both Kin4 and Mck1 work in parallel to counteract MEN activation by the Cdc14 early anaphase release (FEAR) network. We show that Mck1's function in SPOC is mediated by the pre-replication complex protein and mitotic cyclin-dependent kinase (M-Cdk) inhibitor, Cdc6, which is degraded in a Mck1-dependent manner prior to mitosis. Moderate overproduction of Cdc6 phenocopies MCK1 deletion and causes SPOC deficiency via its N-terminal, M-Cdk inhibitory domain. Our data uncover an unprecedented role of GSK-3 kinases in coordinating spindle orientation with cell cycle progression.
000182432 536__ $$0G:(DE-HGF)POF4-311$$a311 - Zellbiologie und Tumorbiologie (POF4-311)$$cPOF4-311$$fPOF IV$$x0
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000182432 650_7 $$2Other$$aCdc6
000182432 650_7 $$2Other$$aMCK1
000182432 650_7 $$2Other$$abudding yeast
000182432 650_7 $$2Other$$acell division
000182432 650_7 $$2Other$$acheckpoint control
000182432 650_7 $$2Other$$amitotic exit
000182432 650_7 $$2NLM Chemicals$$aSaccharomyces cerevisiae Proteins
000182432 650_7 $$0EC 2.7.11.26$$2NLM Chemicals$$aGlycogen Synthase Kinase 3
000182432 650_7 $$0EC 2.7.11.1$$2NLM Chemicals$$aProtein Serine-Threonine Kinases
000182432 650_7 $$2NLM Chemicals$$aCell Cycle Proteins
000182432 650_7 $$2NLM Chemicals$$aCDC14 protein, S cerevisiae
000182432 650_7 $$0EC 3.1.3.48$$2NLM Chemicals$$aProtein Tyrosine Phosphatases
000182432 650_7 $$0EC 2.7.12.1$$2NLM Chemicals$$aMCK1 protein, S cerevisiae
000182432 650_2 $$2MeSH$$aHumans
000182432 650_2 $$2MeSH$$aSaccharomyces cerevisiae Proteins: genetics
000182432 650_2 $$2MeSH$$aGlycogen Synthase Kinase 3: genetics
000182432 650_2 $$2MeSH$$aGlycogen Synthase Kinase 3: metabolism
000182432 650_2 $$2MeSH$$aSpindle Apparatus: metabolism
000182432 650_2 $$2MeSH$$aSaccharomycetales: metabolism
000182432 650_2 $$2MeSH$$aProtein Serine-Threonine Kinases
000182432 650_2 $$2MeSH$$aPhosphorylation
000182432 650_2 $$2MeSH$$aSaccharomyces cerevisiae: genetics
000182432 650_2 $$2MeSH$$aMitosis
000182432 650_2 $$2MeSH$$aCell Cycle Proteins: metabolism
000182432 650_2 $$2MeSH$$aProtein Tyrosine Phosphatases: genetics
000182432 650_2 $$2MeSH$$aProtein Tyrosine Phosphatases: metabolism
000182432 7001_ $$aPolat, Irem$$b1
000182432 7001_ $$0P:(DE-He78)5138c10dcd0901d001d67a31423402b5$$aPereira, Gislene$$b2$$eLast author$$udkfz
000182432 773__ $$0PERI:(DE-600)2630944-0$$a10.1098/rsob.220203$$gVol. 12, no. 11, p. 220203$$n11$$p220203$$tOpen biology$$v12$$x2046-2441$$y2022
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