Overlapping kinetochore targets of CK2 and Aurora B kinases in mitotic regulation

Peng, Yutian; Wong, Catherine C. L.; Nakajima, Yuko; Tyers, Randall G.; Sarkeshik, Ali; Yates, John R.; Drubin, David G.; Barnes, Georjana

doi:10.1091/mbc.e10-11-0915

Cited by 20 publications

(21 citation statements)

References 58 publications

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“…Studies have suggested that Ndc10 is a target of both Ipl1 and casein kinase 2 (CK2) (40,41). Phosphorylations of multiple serine and threonine residues influence Ndc10 localization on the anaphase spindle and targeting to kinetochore.…”

Section: Resultsmentioning

confidence: 99%

Structure of Yeast Kinetochore Ndc10 DNA-binding Domain Reveals Unexpected Evolutionary Relationship to Tyrosine Recombinases

Perriches

Singleton

2012

Journal of Biological Chemistry

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Background: Ndc10 is a DNA-binding protein in yeast that is responsible for centromere formation. Results: The structure of the protein unexpectedly shows that it contains a type IB topoisomerase/-integrase fold. Conclusion:The structure demonstrates how the IB/Int fold has been adapted to a new cellular role. Significance: The structure is the first example of the IB/Int fold being used in a non-catalytic protein.

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Section: Resultsmentioning

confidence: 99%

Structure of Yeast Kinetochore Ndc10 DNA-binding Domain Reveals Unexpected Evolutionary Relationship to Tyrosine Recombinases

Perriches

Singleton

2012

Journal of Biological Chemistry

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“…400 μg of purified proteins was subjected to phosphorylation by Hrr25. Phosphorylated residues of Ede1C (900–1381 aa) were identified by tandem mass spectrometry analysis as previously described (Peng et al, 2011). …”

Section: Methodsmentioning

confidence: 99%

Casein Kinase 1 Promotes Initiation of Clathrin-Mediated Endocytosis

Peng

Grassart

et al. 2015

Developmental Cell

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Summary In budding yeast, over 60 proteins functioning in at least 5 modules are recruited to endocytic sites with predictable order and timing. However, how sites of clathrin-mediated endocytosis are initiated and stabilized is not well understood. Here, the casein kinase 1 (CK1) Hrr25 is shown to be an endocytic protein and to be among the earliest proteins to appear at endocytic sites. Hrr25 absence or overexpression decreases or increases the rate of endocytic site initiation, respectively. Ede1, an early endocytic Eps15-like protein important for endocytic initiation, is an Hrr25 target and is required for Hrr25 recruitment to endocytic sites. Hrr25 phosphorylation of Ede1 is required for Hrr25-Ede1 interaction and promotes efficient initiation of endocytic sites. These observations indicate that Hrr25 kinase and Ede1 cooperate to initiate and stabilize endocytic sites. Analysis of the mammalian homologs CK1δ/ε suggests a conserved role for these protein kinases in endocytic site initiation and stabilization.

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“…Therefore, a unique feature of CENP-C Mif2 or a CENP-C Mif2 -binding protein is important for the interaction of Mub1/Ubr2 with kinetochore particles. However, despite the close association of Mub1/Ubr2 with CENP-C Mif2 , we did not detect ubiquitylation of CENP-C Mif2 or a CENP-C Mif2 mutant allele ([47] and data not shown). Because we could not detect a stable association of Mub1/Ubr2 with endogenous kinetochores, Mub1/Ubr2 likely bind to kinetochore particles during the purification process.…”

Section: Discussionmentioning

confidence: 57%

The Mub1/Ubr2 Ubiquitin Ligase Complex Regulates the Conserved Dsn1 Kinetochore Protein

et al. 2013

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The kinetochore is the macromolecular complex that assembles onto centromeric DNA and orchestrates the segregation of duplicated chromosomes. More than 60 components make up the budding yeast kinetochore, including inner kinetochore proteins that bind to centromeric chromatin and outer proteins that directly interact with microtubules. However, little is known about how these components assemble into a functional kinetochore and whether there are quality control mechanisms that monitor kinetochore integrity. We previously developed a method to isolate kinetochore particles via purification of the conserved Dsn1 kinetochore protein. We find that the Mub1/Ubr2 ubiquitin ligase complex associates with kinetochore particles through the CENP-CMif2 protein. Although Mub1/Ubr2 are not stable kinetochore components in vivo, they regulate the levels of the conserved outer kinetochore protein Dsn1 via ubiquitylation. Strikingly, a deletion of Mub1/Ubr2 restores the levels and viability of a mutant Dsn1 protein, reminiscent of quality control systems that target aberrant proteins for degradation. Consistent with this, Mub1/Ubr2 help to maintain viability when kinetochores are defective. Together, our data identify a previously unknown regulatory mechanism for the conserved Dsn1 kinetochore protein. We propose that Mub1/Ubr2 are part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability.

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Overlapping kinetochore targets of CK2 and Aurora B kinases in mitotic regulation

Cited by 20 publications

References 58 publications

Structure of Yeast Kinetochore Ndc10 DNA-binding Domain Reveals Unexpected Evolutionary Relationship to Tyrosine Recombinases

Structure of Yeast Kinetochore Ndc10 DNA-binding Domain Reveals Unexpected Evolutionary Relationship to Tyrosine Recombinases

Casein Kinase 1 Promotes Initiation of Clathrin-Mediated Endocytosis

The Mub1/Ubr2 Ubiquitin Ligase Complex Regulates the Conserved Dsn1 Kinetochore Protein

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