Zds1 regulates PP2ACdc55 activity and Cdc14 activation during mitotic exit via its Zds_C motif

Calabria, Inés; Baró, Bàrbara; Rodriguez-Rodriguez, José-Antonio; Russiñol, Nuria; Queralt, Ethel

doi:10.1242/jcs.097865

Cited by 13 publications

(15 citation statements)

References 50 publications

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“…producing a colony of small size) and inviable segregants. As previously reported [43], [49], [50], [65], [85], deletion of ZDS1 and ZDS2 decreases spore viability and increases sickness with variable penetrance, whereas deletion of IGO1 and IGO2 is well tolerated. B. Stationary phase cells of meiotic segregants with the indicated genotype that were classified as “healthy” in (A) were spotted on YEPD plates and incubated for 2 days at 25°C and 37°C.…”

Section: Supporting Informationsupporting

confidence: 81%

Budding Yeast Greatwall and Endosulfines Control Activity and Spatial Regulation of PP2ACdc55 for Timely Mitotic Progression

et al. 2013

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Entry into mitosis is triggered by cyclinB/Cdk1, whose activity is abruptly raised by a positive feedback loop. The Greatwall kinase phosphorylates proteins of the endosulfine family and allows them to bind and inhibit the main Cdk1-counteracting PP2A-B55 phosphatase, thereby promoting mitotic entry. In contrast to most eukaryotic systems, Cdc14 is the main Cdk1-antagonizing phosphatase in budding yeast, while the PP2ACdc55 phosphatase promotes, instead of preventing, mitotic entry by participating to the positive feedback loop of Cdk1 activation. Here we show that budding yeast endosulfines (Igo1 and Igo2) bind to PP2ACdc55 in a cell cycle-regulated manner upon Greatwall (Rim15)-dependent phosphorylation. Phosphorylated Igo1 inhibits PP2ACdc55 activity in vitro and induces mitotic entry in Xenopus egg extracts, indicating that it bears a conserved PP2A-binding and -inhibitory activity. Surprisingly, deletion of IGO1 and IGO2 in yeast cells leads to a decrease in PP2A phosphatase activity, suggesting that endosulfines act also as positive regulators of PP2A in yeast. Consistently, RIM15 and IGO1/2 promote, like PP2ACdc55, timely entry into mitosis under temperature-stress, owing to the accumulation of Tyr-phosphorylated Cdk1. In addition, they contribute to the nuclear export of PP2ACdc55, which has recently been proposed to promote mitotic entry. Altogether, our data indicate that Igo proteins participate in the positive feedback loop for Cdk1 activation. We conclude that Greatwall, endosulfines, and PP2A are part of a regulatory module that has been conserved during evolution irrespective of PP2A function in the control of mitosis. However, this conserved module is adapted to account for differences in the regulation of mitotic entry in different organisms.

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Section: Supporting Informationsupporting

confidence: 81%

Budding Yeast Greatwall and Endosulfines Control Activity and Spatial Regulation of PP2ACdc55 for Timely Mitotic Progression

et al. 2013

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“…Although the molecular details are poorly understood, it is believed that proteins like Separase and nuclear export Zds1 and Zds2 are able to downregulate PP2A prior to mitotic exit ( Calabria et al, 2012 ). The subsequent depletion of Cdk1, as cell cycle progresses to late anaphase, could trigger the MEN pathway, which is activated to achieve full Cdc14 phosphatase activity.…”

Section: Function Of Phosphatases In Mitotic Exitmentioning

confidence: 99%

Protein Phosphatases Involved in Regulating Mitosis: Facts and Hypotheses

Kim¹,

Fernandes²,

Lee³

2016

Molecules and Cells

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Almost all eukaryotic proteins are subject to post-translational modifications during mitosis and cell cycle, and in particular, reversible phosphorylation being a key event. The recent use of high-throughput experimental analyses has revealed that more than 70% of all eukaryotic proteins are regulated by phosphorylation; however, the mechanism of dephosphorylation, counteracting phosphorylation, is relatively unknown. Recent discoveries have shown that many of the protein phosphatases are involved in the temporal and spatial control of mitotic events, such as mitotic entry, mitotic spindle assembly, chromosome architecture changes and cohesion, and mitotic exit. This implies that certain phosphatases are tightly regulated for timely dephosphorylation of key mitotic phosphoproteins and are essential for control of various mitotic processes. This review describes the physiological and pathological roles of mitotic phosphatases, as well as the versatile role of various protein phosphatases in several mitotic events.

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“…They probably accomplish this by binding and retaining PP2A Cdc55 in the cytoplasm, thereby lowering its nuclear concentration (Rossio and Yoshida 2011), but the precise mechanism remains unclear. Analysis of their localization in isolated nucleoli suggests that Zds proteins may regulate a nucleolar pool of the phosphatase (Calabria et al 2012).…”

Section: Fear Pathwaymentioning

confidence: 99%

Mitotic Exit and Separation of Mother and Daughter Cells

2012

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Productive cell proliferation involves efficient and accurate splitting of the dividing cell into two separate entities. This orderly process reflects coordination of diverse cytological events by regulatory systems that drive the cell from mitosis into G1. In the budding yeast Saccharomyces cerevisiae, separation of mother and daughter cells involves coordinated actomyosin ring contraction and septum synthesis, followed by septum destruction. These events occur in precise and rapid sequence once chromosomes are segregated and are linked with spindle organization and mitotic progress by intricate cell cycle control machinery. Additionally, critical parts of the mother/daughter separation process are asymmetric, reflecting a form of fate specification that occurs in every cell division. This chapter describes central events of budding yeast cell separation, as well as the control pathways that integrate them and link them with the cell cycle.

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Zds1 regulates PP2ACdc55 activity and Cdc14 activation during mitotic exit via its Zds_C motif

Cited by 13 publications

References 50 publications

Budding Yeast Greatwall and Endosulfines Control Activity and Spatial Regulation of PP2ACdc55 for Timely Mitotic Progression

Budding Yeast Greatwall and Endosulfines Control Activity and Spatial Regulation of PP2ACdc55 for Timely Mitotic Progression

Protein Phosphatases Involved in Regulating Mitosis: Facts and Hypotheses

Mitotic Exit and Separation of Mother and Daughter Cells

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