Dataset Information


A common molecular mechanism underlies the role of Mps1 in chromosome biorientation and the spindle assembly checkpoint

ABSTRACT: The conserved Mps1 kinase corrects improper kinetochore-microtubule attachments, thereby ensuring chromosome biorientation. Yet, its critical targets in this process remain elusive. Mps1 is also involved in the spindle assembly checkpoint (SAC), the surveillance mechanism halting chromosome segregation until biorientation is attained. Its role in SAC activation is antagonized by the PP1 phosphatase and involves phosphorylation of Knl1/Spc105, which recruits Bub1 to kinetochores to promote assembly of SAC effector complexes. A crucial question is whether error correction and SAC activation are part of a single device or separable pathways. Here we characterise a novel yeast mutant, mps1-3, defective in chromosome biorientation and SAC activation. Through an unbiased screen for suppressors, we found that mutations lowering PP1 levels at Spc105 or forced association of Bub1 with Spc105 reinstate both chromosome biorientation and SAC signalling in mps1-3 cells. Our data strongly argue that Mps1-dependent phosphorylation of the Knl1/Spc105 kinetochore scaffold is critical for Mps1 function in both chromosome biorientation and SAC activation, thus supporting the idea that a common sensory apparatus simultaneously elicits error correction and SAC signalling. Overall design: ChIP-seq analysis to study the centromeric localization of Mps1 in the mps1-3 mutant and in the external suppressors spc105-18 mps1-3 and GLC7-24 mps1-3. Mps1 and Mps1-3 have been tagged at the C-ter of the protein with 3HA (3-Hemagglutinin)

INSTRUMENT(S): Illumina HiSeq 2000 (Saccharomyces cerevisiae)

ORGANISM(S): Saccharomyces cerevisiae  

SUBMITTER: Giorgia Benzi  

PROVIDER: GSE144741 | GEO | 2020-02-05


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