Defects in Saccharomyces cerevisiae protein phosphatase type I activate the spindle/kinetochore checkpoint

Bloecher, Andrew; Tatchell, Kelly

doi:10.1101/gad.13.5.517

Cited by 56 publications

(52 citation statements)

References 39 publications

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“…In human cells, the amounts of Plk1 protein and its kinase activity peak at mitosis (18). During mitosis, Plk1 transiently associates with mitotic structures such as the spindle apparatus, kinetochores, and centrosomes (20). Recent studies have shown that Plk1 contributes to a variety of mitotic (or meiotic) events, including activation of cyclin B-Cdc2, breakdown of the nuclear membrane, centrosome maturation, and formation of the bipolar spindle at the onset of mitosis (21)(22)(23).…”

mentioning

confidence: 99%

Reactive Oxygen Species-induced Phosphorylation of p53 on Serine 20 Is Mediated in Part by Polo-like Kinase-3

Xie

Wang

et al. 2001

Journal of Biological Chemistry

133

114

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mentioning

confidence: 99%

Reactive Oxygen Species-induced Phosphorylation of p53 on Serine 20 Is Mediated in Part by Polo-like Kinase-3

Xie

Wang

et al. 2001

Journal of Biological Chemistry

133

114

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“…Experimental evidence indicates that the conserved type 1 protein phosphatase PP1 carries out this role. Mutations in the yeast PP1 gene, GLC7, suppress the temperature sensitivity of ipl1 mutants (12)(13)(14), activate the spindle assembly checkpoint (15,16), and reduce the affinity of microtubules for kinetochore complexes (16). GLC7 mutations also enhance the phosphorylation state of the Ipl1 substrates, histone H3 (13), and Dam1 (14).…”

mentioning

confidence: 99%

Temperature-sensitive ipl1-2/Aurora B mutation is suppressed by mutations in TOR complex 1 via the Glc7/PP1 phosphatase

Tatchell

Makrantoni

Stark

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Ipl1/Aurora B is the catalytic subunit of a complex that is required for chromosome segregation and nuclear division. Before anaphase, Ipl1 localizes to kinetochores, where it is required to establish proper kinetochore-microtubule associations and regulate the spindle assembly checkpoint. The protein phosphatase Glc7/ PP1 opposes Ipl1 for some of these activities. To more thoroughly characterize the Glc7 phosphatase that opposes Ipl1, we have identified mutations that suppress the thermosensitivity of an ipl1-2 mutant. In addition to mutations in genes previously associated with ipl1 suppression, we recovered a null mutant in TCO89, which encodes a subunit of the TOR complex 1 (TORC1), the conserved rapamycin-sensitive kinase activity that regulates cell growth in response to nutritional status. The temperature sensitivity of ipl1-2 can also be suppressed by null mutation of TOR1 or by administration of pharmacological TORC1 inhibitors, indicating that reduced TORC1 activity is responsible for the suppression. Suppression of the ipl1-2 growth defect is accompanied by increased fidelity of chromosome segregation and increased phosphorylation of the Ipl1 substrates histone H3 and Dam1. Nuclear Glc7 levels are reduced in a tco89 mutant, suggesting that TORC1 activity is required for the nuclear accumulation of Glc7. In addition, several mutant GLC7 alleles that suppress the temperature sensitivity of ipl1-2 exhibit negative synthetic genetic interactions with TORC1 mutants. Together, our results suggest that TORC1 positively regulates the Glc7 activity that opposes Ipl1 and provide a mechanism to tie nutritional status with mitotic regulation.

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“…Reduction of Glc7 activity causes cell cycle arrest at the spindle assembly checkpoint (61,62). Depletion of Glc8 in glc7-R121K cells appears to cause the same block in the cell cycle because they arrest as large budded cells with replicated chromosomes.…”

Section: Pho85 Phosphorylates Glc8mentioning

confidence: 95%

Pho85 Phosphorylates the Glc7 Protein Phosphatase Regulator Glc8 in Vivo

Tan¹,

Morcos²,

Cannon

2003

Journal of Biological Chemistry

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The budding yeast Glc7 serine/threonine protein phosphatase-1 is regulated by Glc8, the yeast ortholog of mammalian phosphatase inhibitor-2. In this work, we demonstrated that similarly to inhibitor-2, Glc8 function is regulated by phosphorylation. The cyclindependent protein kinase, Pho85, in conjunction with the related cyclins Pcl6 and Pcl7 comprise the major Glc8 kinase in vivo and in vitro. Several glc7 mutations are dependent on the presence of Glc8 for viability. For example, glc7 alleles R121K, R142H, and R198D are lethal in combination with a glc8 deletion. We found that glc7-R121K is lethal in combination with a pho85 deletion. This finding indicates that Pho85 is the sole Glc8 kinase in vivo. Furthermore, glc7-R121K is also lethal when combined with deletions of pcl6, plc7, pcl8, and pcl10, indicating that these related cyclins redundantly activate Pho85 for Glc8 phosphorylation in vivo. In vitro kinase assays and genetic results indicate that Pho85 cyclins Pcl6 and Pcl7 comprise the predominant Glc8 kinase.

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Defects in Saccharomyces cerevisiae protein phosphatase type I activate the spindle/kinetochore checkpoint

Cited by 56 publications

References 39 publications

Reactive Oxygen Species-induced Phosphorylation of p53 on Serine 20 Is Mediated in Part by Polo-like Kinase-3

Reactive Oxygen Species-induced Phosphorylation of p53 on Serine 20 Is Mediated in Part by Polo-like Kinase-3

Temperature-sensitive ipl1-2/Aurora B mutation is suppressed by mutations in TOR complex 1 via the Glc7/PP1 phosphatase

Pho85 Phosphorylates the Glc7 Protein Phosphatase Regulator Glc8 in Vivo

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