Aurora Kinase A Is Not Involved in CPEB1 Phosphorylation and cyclin B1 mRNA Polyadenylation during Meiotic Maturation of Porcine Oocytes

Komrskova, Pavla; Šušor, Andrej; Malı́k, Radek; Prochazkova, Barbora; Lišková, Lucie; Supolikova, Jaroslava; Hladky, Stepan; Kubelka, Michal

doi:10.1371/journal.pone.0101222

Cited by 26 publications

(25 citation statements)

References 54 publications

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“…The CPEB2 protein was stable until metaphase I, when its partial degradation occurred. This matches with its paralog CPEB1, the degradation of which is necessary for the transition between metaphase I and metaphase II in Xenopus oocytes [ 19 ], and which has also been observed also in porcine oocytes [ 38 ]. Mendez et al [ 19 ] reported similar results, suggesting that the degradation of CPEB1 is necessary for the transition between metaphase I and metaphases II in Xenopus oocytes.…”

Section: Discussionsupporting

confidence: 67%

CPEB2 Is Necessary for Proper Porcine Meiotic Maturation and Embryonic Development

Prochazkova

Komrskova

Kubelka

2018

IJMS

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Oocyte meiotic maturation and embryogenesis are some of the most important physiological processes that occur in organisms, playing crucial roles in the preservation of life in all species. The post-transcriptional regulation of maternal messenger ribonucleic acids (mRNAs) and the post-translational regulation of proteins are critical in the control of oocyte maturation and early embryogenesis. Translational control affects the basic mechanism of protein synthesis, thus, knowledge of the key components included in this machinery is required in order to understand its regulation. Cytoplasmic polyadenylation element binding proteins (CPEBs) bind to the 3′-end of mRNAs to regulate their localization and translation and are necessary for proper development. In this study we examined the expression pattern of cytoplasmic polyadenylation element binding protein 2 (CPEB2) both on the mRNA (by real-time quantitative reverse transcription polymerase chain reaction, qRT-PCR) and protein (by Western blotting, WB) level, as well as its localization during the meiotic maturation of porcine oocytes and early embryonic development by immunocytochemistry (ICC). For the elucidation of its functions, CPEB2 knockdown by double-strand RNA (dsRNA) was used. We discovered that CPEB2 is expressed during all stages of porcine meiotic maturation and embryonic development. Moreover, we found that it is necessary to enable a high percentage of oocytes to reach the metaphase II (MII) stage, as well as for the production of good-quality parthenogenetic blastocysts.

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Section: Discussionsupporting

confidence: 67%

CPEB2 Is Necessary for Proper Porcine Meiotic Maturation and Embryonic Development

Prochazkova

Komrskova

Kubelka

2018

IJMS

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“…In contrast with mitotic cell cycles, this transition has not been reported to require cyclin A (Kobayashi et al, 1991;Minshull et al, 1991;Okano-Uchida et al, 1998;Nebreda and Ferby, 2000;Kishimoto, 2003Kishimoto, , 2018. Furthermore, Plk1 (Pahlavan et al, 2000;Okano-Uchida et al, 2003;Gaffré et al, 2011) and Aurora (Maton et al, 2003;Abe et al, 2010;Komrskova et al, 2014) are nonessential for transition in some oocytes. Thus, mechanisms other than the cyclin A-Cdk1/Plk1 axis likely trigger cyclin B-Cdk1 activation in oocytes.…”

Section: Introductionmentioning

confidence: 87%

SGK phosphorylates Cdc25 and Myt1 to trigger cyclin B–Cdk1 activation at the meiotic G2/M transition

Hiraoka

Hosoda

Chiba

et al. 2019

Journal of Cell Biology

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The kinase cyclin B–Cdk1 complex is a master regulator of M-phase in both mitosis and meiosis. At the G2/M transition, cyclin B–Cdk1 activation is initiated by a trigger that reverses the balance of activities between Cdc25 and Wee1/Myt1 and is further accelerated by autoregulatory loops. In somatic cell mitosis, this trigger was recently proposed to be the cyclin A–Cdk1/Plk1 axis. However, in the oocyte meiotic G2/M transition, in which hormonal stimuli induce cyclin B–Cdk1 activation, cyclin A–Cdk1 is nonessential and hence the trigger remains elusive. Here, we show that SGK directly phosphorylates Cdc25 and Myt1 to trigger cyclin B–Cdk1 activation in starfish oocytes. Upon hormonal stimulation of the meiotic G2/M transition, SGK is activated by cooperation between the Gβγ-PI3K pathway and an unidentified pathway downstream of Gβγ, called the atypical Gβγ pathway. These findings identify the trigger in oocyte meiosis and provide insights into the role and activation of SGK.

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“…The mechanisms of temporal and selective activation of maternal mRNAs are complicated and diverse among species (Komrskova et al, 2014). Cytoplasmic polyadenylation of the 3′-untranslated region (3′-UTR) is largely correlated with mRNA stability and translational activation of mRNA, and plays an essential role in oocyte maturation.…”

Section: Introductionmentioning

confidence: 99%

A MAPK cascade couples maternal mRNA translation and degradation to meiotic cell cycle progression in mouse oocytes

et al. 2017

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Mammalian oocyte maturation depends on the translational activation of stored maternal mRNAs upon meiotic resumption. Cytoplasmic polyadenylation element binding protein 1 (CPEB1) is a key oocyte factor that regulates maternal mRNA translation. However, the signal that triggers CPEB1 activation at the onset of mammalian oocyte maturation is not known. We provide evidence that a mitogen-activated protein kinase (MAPK) cascade couples maternal mRNA translation to meiotic cell cycle progression in mouse oocytes by triggering CPEB1 phosphorylation and degradation. Mutations of the phosphorylation sites or ubiquitin E3 ligase binding sites in CPEB1 have a dominant-negative effect in oocytes, and mimic the phenotype of ERK1/2 knockout, by impairing spindle assembly and mRNA translation. Overexpression of the CPEB1 downstream translation activator DAZL in ERK1/2-deficient oocytes partially rescued the meiotic defects, indicating that ERK1/2 is essential for spindle assembly, metaphase II arrest and maternal-zygotic transition (MZT) primarily by triggering the translation of key maternal mRNAs. Taken together, ERK1/2-mediated CPEB1 phosphorylation/degradation is a major mechanism of maternal mRNA translational activation, and is crucial for mouse oocyte maturation and MZT.

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Aurora Kinase A Is Not Involved in CPEB1 Phosphorylation and cyclin B1 mRNA Polyadenylation during Meiotic Maturation of Porcine Oocytes

Cited by 26 publications

References 54 publications

CPEB2 Is Necessary for Proper Porcine Meiotic Maturation and Embryonic Development

CPEB2 Is Necessary for Proper Porcine Meiotic Maturation and Embryonic Development

SGK phosphorylates Cdc25 and Myt1 to trigger cyclin B–Cdk1 activation at the meiotic G2/M transition

A MAPK cascade couples maternal mRNA translation and degradation to meiotic cell cycle progression in mouse oocytes

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