Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A–Cdc55 at anaphase onset

Játiva, Soraya; Calabria, Inés; Moyano-Rodríguez, Yolanda; Garcia, Patrícia Salomão; Queralt, Ethel

doi:10.1007/s00018-019-03086-5

Cited by 12 publications

(15 citation statements)

References 72 publications

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“…At anaphase onset, PP2A-Cdc55 is downregulated in a separase-dependent manner in cooperation with Zds1/Zds2 [64]. Finally, during anaphase, Clb2-Cdk1 promotes Cdc55 subunit phosphorylation to inhibit the phosphatase activity of PP2A and, once that the spindle is properly positioned, cells initiate mitotic exit signaling [52,70,71].…”

Section: Cdc14 and The Regulation Of The Cell Cyclementioning

confidence: 99%

“…Cdc14 further participates in the DNA damage response by anchoring DNA lesions to the SPBs, in this way facilitating their repair [51]. In anaphase, Cdc55 phosphorylation by Cdk1-Clb2 stimulates full Net1/Cfi1 and Cdc14 disassociation and, subsequently, completes Cdc14 activation (inhibitory red line) [52]. The final release of Cdc14 to the cytoplasm globally reverses Cdk activity in coordination with PPA2-Cdc55 and PPA2-Rts1 phosphatases, supporting exit from mitosis [53].…”

Section: Introductionmentioning

confidence: 99%

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The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control

Manzano-López

Monje-Casas

2020

IJMS

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The Cdc14 phosphatase is a key regulator of mitosis in the budding yeast Saccharomyces cerevisiae. Cdc14 was initially described as playing an essential role in the control of cell cycle progression by promoting mitotic exit on the basis of its capacity to counteract the activity of the cyclin-dependent kinase Cdc28/Cdk1. A compiling body of evidence, however, has later demonstrated that this phosphatase plays other multiple roles in the regulation of mitosis at different cell cycle stages. Here, we summarize our current knowledge about the pivotal role of Cdc14 in cell cycle control, with a special focus in the most recently uncovered functions of the phosphatase.

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Section: Cdc14 and The Regulation Of The Cell Cyclementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control

Manzano-López

Monje-Casas

2020

IJMS

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“…Human PP2A catalytic subunit phosphorylation at its C-terminal tail at Thr307 prevented binding of B55 [104]. A recent study reported that phosphorylation of Thr174 of the budding yeast B55 by mitotic Cdk led to inhibition of its phosphatase activity [105]. Phosphorylation of the equivalent site Ser167 on human B55α, possibly by Cdk1-Cyclin B, inhibits holoenzyme assembly [106].…”

Section: G2/m Transitionmentioning

confidence: 99%

Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis

Kataria

Yamano

2019

Cells

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Accurate division of cells into two daughters is a process that is vital to propagation of life. Protein phosphorylation and selective degradation have emerged as two important mechanisms safeguarding the delicate choreography of mitosis. Protein phosphatases catalyze dephosphorylation of thousands of sites on proteins, steering the cells through establishment of the mitotic phase and exit from it. A large E3 ubiquitin ligase, the anaphase-promoting complex/cyclosome (APC/C) becomes active during latter stages of mitosis through G1 and marks hundreds of proteins for destruction. Recent studies have revealed the complex interregulation between these two classes of enzymes. In this review, we highlight the direct and indirect mechanisms by which phosphatases and the APC/C mutually influence each other to ensure accurate spatiotemporal and orderly progression through mitosis, with a particular focus on recent insights and conceptual advances.

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“…In metaphase, Net1 is maintained in an under-phosphorylated state by the phosphatase PP2A-Cdc55. At anaphase onset, separase, together with Zds1/2 proteins, promotes the PP2A-Cdc55 inactivation via the Cdk1-dependent phosphorylation of the Cdc55 regulatory subunit, allowing the accumulation of phosphorylated Net1 isoforms [ 96 , 98 , 100 , 101 ]. Increase levels of phosphorylated Net1 by Cdk1-Clb2, with the contribution of the polo-like kinase Cdc5, stimulates Cdc14 release from the nucleolus since the phosphorylated form of Net1 has lower affinity toward Cdc14 [ 93 – 96 , 102 ].…”

Section: Introductionmentioning

confidence: 99%

“…When cells reach anaphase with a correct aligned mitotic spindle, Cdc5 phosphorylates Bfa1 and inactivates Bfa1-Bub2 GAP [ 115 , 116 ]. In addition, Cdk1-dependent PP2A-Cdc55 inhibition at early anaphase [ 96 , 101 ] also promotes the accumulation of phosphorylated Cdc5-dependent Bfa1. Active Tem1 interacts with and activates the Pak-like kinase Cdc15 [ 117 , 118 ].…”

Section: Introductionmentioning

confidence: 99%

The regulation of Net1/Cdc14 by the Hog1 MAPK upon osmostress unravels a new mechanism regulating mitosis

et al. 2020

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During evolution, cells have developed a plethora of mechanisms to optimize survival in a changing and unpredictable environment. In this regard, they have evolved networks that include environmental sensors, signaling transduction molecules and response mechanisms. Hog1 (yeast) and p38 (mammals) stress-activated protein kinases (SAPKs) are activated upon stress and they drive a full collection of cell adaptive responses aimed to maximize survival. SAPKs are extensively used to learn about the mechanisms through which cells adapt to changing environments. In addition to regulating gene expression and metabolism, SAPKs control cell cycle progression. In this review, we will discuss the latest findings related to the SAPK-driven regulation of mitosis upon osmostress in yeast.

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Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A–Cdc55 at anaphase onset

Cited by 12 publications

References 72 publications

The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control

The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control

Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis

The regulation of Net1/Cdc14 by the Hog1 MAPK upon osmostress unravels a new mechanism regulating mitosis

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