MPF and the Control of Meiotic Divisions: Old Problems, New Concepts

Jessus, Catherine

doi:10.1002/9780470687970.ch9

Cited by 4 publications

(5 citation statements)

References 224 publications

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“…Cdk1 and the kinases activated under its control (Mos/MAPK, Aurora-A, Plk1, etc.) trigger a second wave of protein translation and accumulation, as well as mediating the structural changes of cell division: NEBD, chromosome condensation and formation of the Meiosis I spindle (Jessus, 2010;Santoni et al, 2024). They also activate the anaphase-promoting complex (APC), an E3 ubiquitin ligase, leading to the degradation of both Cyclin B and securin, thus enabling entry into anaphase I and chromosome separation and the expulsion of the 1 st polar body (Fig.…”

Section: Introductionmentioning

confidence: 99%

“…These events trigger the entry into metaphase II and the formation of the MII spindle. In all vertebrates as a result of the stabilization of cyclin B oocytes arrest in the middle of the meiotic division due to the stabilization of B-Cyclins, resulting from APC inhibition by the Emi2/Erp1 (Jessus, 2010) (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

“…The newly synthesized B1-Cyclins bind to monomeric Cdk1 to form a small pool of active complexes that evade the inhibition of Myt1 (Hochegger et al, 2001;Gaffré et al, 2011). Subsequently, this small amount of active Cdk1 initiates a complex network of feedback loops, involving many kinases and phosphatases, thereby creating an auto-amplification loop (Jessus, 2010) (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

“…1). Within this loop, the activation of the Cdc25 phosphatase that dephosphorylates Cdk1 and the inhibition of the PP2A phosphatase that counteracts Cdk1, lead to a rapid and full activation of Cdk1-Cyclin B (Jessus, 2010;Lemonnier et al, 2020). Another important player in this positive feedback loop is Mos, whose translation is induced by progesterone and which accumulates at the time of Cdk1 activation (Sagata et al, 1988(Sagata et al, , 1989aFrank-Vaillant et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

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Decoding protein phosphorylation during oocyte meiotic divisions using phosphoproteomics

Peshkin,

Daldello,

Van Itallie

et al. 2024

Preprint

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Oocyte meiotic divisions represent a critical process in sexual reproduction, as a diploid non-dividing oocyte is transformed into a haploid fertilizable egg, as a prelude for the subsequent embryonic divisions and differentiation. Although cell differentiation and proliferation are governed by transcription, oocyte maturation and early embryonic divisions depend entirely on changes in protein abundance and post-translational modifications. Here, we analyze the abundance and phosphorylation of proteins during Xenopus oocyte meiotic maturation. We reveal significant shifts in protein stability, related to spindle assembly, DNA replication and RNA-binding. Our analysis pinpoints broad changes in phosphorylation correlating with key cytological meiotic milestones, noteworthy changes in membrane trafficking, nuclear envelope disassembly and modifications in microtubule dynamics. Additionally, specific phosphorylation events target regulators of protein translation, Cdk1 and the Mos/MAPK pathway, thereby providing insight into the dynamics of Cdk1 activity, as related to the meiotic cell cycle. This study sheds light on the orchestration of protein dynamics and phosphorylation events during oocyte meiotic divisions, providing a rich resource for understanding the molecular pathways orchestrating meiotic progression in the frog, and most likely applicable to other vertebrate species.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Decoding protein phosphorylation during oocyte meiotic divisions using phosphoproteomics

Peshkin,

Daldello,

Van Itallie

et al. 2024

Preprint

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“…); their huge amounts (thousands of them per ovary) as well as their high protein content (30 µg of soluble proteins per oocyte) allows biochemical and proteomic approaches. Thanks to the biochemistry of oocytes, and especially amphibian oocytes, a number of mitotic regulators have been discovered, starting with MPF itself [16][17][18]. In this model system, the G2-to-M transition can be considered as a 3-step process.…”

Section: Introductionmentioning

confidence: 99%

The G2-to-M transition from a phosphatase perspective: a new vision of the meiotic division

2020

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Cell division is orchestrated by the phosphorylation and dephosphorylation of thousands of proteins. These posttranslational modifications underlie the molecular cascades converging to the activation of the universal mitotic kinase, Cdk1, and entry into cell division. They also govern the structural events that sustain the mechanics of cell division. While the role of protein kinases in mitosis has been well documented by decades of investigations, little was known regarding the control of protein phosphatases until the recent years. However, the regulation of phosphatase activities is as essential as kinases in controlling the activation of Cdk1 to enter M-phase. The regulation and the function of phosphatases result from post-translational modifications but also from the combinatorial association between conserved catalytic subunits and regulatory subunits that drive their substrate specificity, their cellular localization and their activity. It now appears that sequential dephosphorylations orchestrated by a network of phosphatase activities trigger Cdk1 activation and then order the structural events necessary for the timely execution of cell division. This review discusses a series of recent works describing the important roles played by protein phosphatases for the proper regulation of meiotic division. Many breakthroughs in the field of cell cycle research came from studies on oocyte meiotic divisions. Indeed, the meiotic division shares most of the molecular regulators with mitosis. The natural arrests of oocytes in G2 and in M-phase, the giant size of these cells, the variety of model species allowing either biochemical or imaging as well as genetics approaches explain why the process of meiosis has served as an historical model to decipher signalling pathways involved in the G2-to-M transition. The review especially highlights how the phosphatase PP2A-B55δ critically orchestrates the timing of meiosis resumption in amphibian oocytes. By opposing the kinase PKA, PP2A-B55δ controls the release of the G2 arrest through the dephosphorylation of their substrate, Arpp19. Few hours later, the inhibition of PP2A-B55δ by Arpp19 releases its opposing kinase, Cdk1, and triggers M-phase. In coordination with a variety of phosphatases and kinases, the PP2A-B55δ/Arpp19 duo therefore emerges as the key effector of the G2-to-M transition.

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Greatwall Kinase, ARPP-19 and Protein Phosphatase 2A: Shifting the Mitosis Paradigm

Haccard

Jessus

2011

Results and Problems in Cell Differentiation

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Control of entry into mitosis has long been seen in terms of an explosive activation of cyclin-dependent kinase 1, the mitotic driver ensuring the phosphorylation of hundreds of proteins required for cell division. However, if these phosphorylations are maintained during M-phase, they must be removed when cells exit mitosis. It has been surmised that an "antimitotic" phosphatase must be inhibited to allow mitosis entry and activated for returning to interphase. This chapter discusses a series of recent works conducted on Xenopus egg extracts that provide the answers regarding the identity and the regulation of such a phosphatase. PP2A-B55δ is the major phosphatase controlling exit from mitosis; it is negatively regulated by the kinase Greatwall that phosphorylates the small protein ARPP-19 and converts it into a potent PP2A inhibitor. These findings provide a new element of paramount importance in the control of mitosis.

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MPF and the Control of Meiotic Divisions: Old Problems, New Concepts

Cited by 4 publications

References 224 publications

Decoding protein phosphorylation during oocyte meiotic divisions using phosphoproteomics

Decoding protein phosphorylation during oocyte meiotic divisions using phosphoproteomics

The G2-to-M transition from a phosphatase perspective: a new vision of the meiotic division

Greatwall Kinase, ARPP-19 and Protein Phosphatase 2A: Shifting the Mitosis Paradigm

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