Comparative genetic analysis of PP2A-Cdc55 regulators in budding yeast

Rossio, Valentina; Kazatskaya, Anna; Hirabayashi, Mayo; Yoshida, Satoshi

doi:10.4161/cc.29064

Cited by 10 publications

(11 citation statements)

References 38 publications

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“…In this context, overexpression of Zds can sequestrate PP2A-Cdc55 in the cytoplasm and promote precocious mitotic entry. On the other hand, Igo1/2 control nuclear accumulation of PP2A-Cdc55 supporting the idea that Igo1/2 inhibit nuclear PP2A-Cdc55 by direct binding (Bontron et al, 2013;Rossio et al, 2014).…”

Section: Greatwall Regulates Both Mitosis and Meiosis 249supporting

confidence: 59%

The master Greatwall kinase, a critical regulator of mitosis and meiosis

Vigneron¹,

Robert²,

Hached³

et al. 2016

Int. J. Dev. Biol.

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Entry into mitosis requires the coordinated activation of various protein kinases and phosphatases that together activate sequential signaling pathways allowing entry, progression and exit of mitosis. The limiting step is thought to be the activation of the mitotic Cdk1-cyclin B kinase. However, this model has recently evolved with new data showing that in addition to the Cdk1-cyclin B complex, Greatwall (Gwl) kinase is also required to enter into and maintain mitosis. This new concept proposes that entry into mitosis is now based on the combined activation of both kinases Cdk1-cyclin B and Gwl, the former promoting massive phosphorylation of mitotic substrates and the latter inhibiting PP2A-B55 phosphatase responsible for dephosphorylation of these substrates. Activated Gwl phosphorylates both Arpp19 and ENSA, which associate and inhibit PP2A-B55. This pathway seems relatively well conserved from yeast to humans, although some differences appear based on models or techniques used. While Gwl is activated by phosphorylation, its inactivation requires dephosphorylation of critical residues. Several phosphatases such as PP1, PP2A-B55 and FCP1 are required to control the dephosphorylation and inactivation of Gwl and a properly regulated mitotic exit. Gwl has also been reported to be involved in cancer processes and DNA damage recovery. These new findings support the idea that the Gwl-Arpp19/ENSA-PP2A-B55 pathway is essential to achieve an efficient division of cells and to maintain genomic stability.

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Section: Greatwall Regulates Both Mitosis and Meiosis 249supporting

confidence: 59%

The master Greatwall kinase, a critical regulator of mitosis and meiosis

Vigneron¹,

Robert²,

Hached³

et al. 2016

Int. J. Dev. Biol.

View full text Add to dashboard Cite

show abstract

“…The difference in localization suggests that Igo1/2 and Zds1/2 proteins control distinct functions of PP2A Cdc55 and do so by different mechanisms. Zds proteins, however, play a major role in the inhibition of PP2A Cdc55 in early mitosis, when compared to the endosulfine proteins [117].…”

Section: Pp2a and Pp2a-like Phosphatasesmentioning

confidence: 99%

Ser/Thr protein phosphatases in fungi: structure, regulation and function

2019

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Reversible phospho-dephosphorylation of proteins is a major mechanism for the control of cellular functions. By large, Ser and Thr are the most frequently residues phosphorylated in eukar-yotes. Removal of phosphate from these amino acids is catalyzed by a large family of well-conserved enzymes, collectively called Ser/Thr protein phosphatases. The activity of these enzymes has an enormous impact on cellular functioning. In this work we pre-sent the members of this family in S. cerevisiae and other fungal species, and review the most recent findings concerning their regu-lation and the roles they play in the most diverse aspects of cell biology.

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“…Interestingly, in this context, Xenopus , Drosophila and likely human cells employ their respective greatwall kinase pathway (Gwl-endosulfine-B55) to maintain high-level phosphorylation of cyclin B-CDK1 substrates, thereby promoting mitotic entry 26 27 . In yeast, however, the Gwl signalling branch contributes only marginally to the regulation of mitotic entry 28 29 , likely because TORC1 curtails signalling through Rim15 in exponentially growing cells.…”

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confidence: 99%

TORC1 controls G1–S cell cycle transition in yeast via Mpk1 and the greatwall kinase pathway

2015

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The target of rapamycin complex 1 (TORC1) pathway couples nutrient, energy and hormonal signals with eukaryotic cell growth and division. In yeast, TORC1 coordinates growth with G1–S cell cycle progression, also coined as START, by favouring the expression of G1 cyclins that activate cyclin-dependent protein kinases (CDKs) and by destabilizing the CDK inhibitor Sic1. Following TORC1 downregulation by rapamycin treatment or nutrient limitation, clearance of G1 cyclins and C-terminal phosphorylation of Sic1 by unknown protein kinases are both required for Sic1 to escape ubiquitin-dependent proteolysis prompted by its flagging via the SCFCdc4 (Skp1/Cul1/F-box protein) ubiquitin ligase complex. Here we show that the stabilizing phosphorylation event within the C-terminus of Sic1 requires stimulation of the mitogen-activated protein kinase, Mpk1, and inhibition of the Cdc55 protein phosphatase 2A (PP2ACdc55) by greatwall kinase-activated endosulfines. Thus, Mpk1 and the greatwall kinase pathway serve TORC1 to coordinate the phosphorylation status of Sic1 and consequently START with nutrient availability.

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Comparative genetic analysis of PP2A-Cdc55 regulators in budding yeast

Cited by 10 publications

References 38 publications

The master Greatwall kinase, a critical regulator of mitosis and meiosis

The master Greatwall kinase, a critical regulator of mitosis and meiosis

Ser/Thr protein phosphatases in fungi: structure, regulation and function

TORC1 controls G1–S cell cycle transition in yeast via Mpk1 and the greatwall kinase pathway

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