scholarly journals Decision letter: Control of PNG kinase, a key regulator of mRNA translation, is coupled to meiosis completion at egg activation

2016 ◽  
Keyword(s):  
Mrna Translation ◽  
Egg Activation ◽  
Kinase A

scholarly journals The GNU subunit of PNG kinase, the developmental regulator of mRNA translation, binds BIC-C to localize to RNP granules

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Emir E Avilés-Pagán ◽  
Masatoshi Hara ◽  
Terry L Orr-Weaver
Keyword(s):  
Translational Regulation ◽  
Mrna Translation ◽  
Mature Oocyte ◽  
Early Embryogenesis ◽  
Egg Activation ◽  
Maternal Mrna ◽  
Rnp Granules

Control of mRNA translation is a key mechanism by which the differentiated oocyte transitions to a totipotent embryo. In Drosophila, the PNG kinase complex regulates maternal mRNA translation at the oocyte-to-embryo transition. We previously showed the GNU activating subunit is crucial in regulating PNG and timing its activity to the window between egg activation and early embryogenesis (Hara et al., 2017). In this study, we find associations between GNU and proteins of RNP granules and demonstrate that GNU localizes to cytoplasmic RNP granules in the mature oocyte, identifying GNU as a new component of a subset of RNP granules. Furthermore, we define roles for the domains of GNU. Interactions between GNU and the granule component BIC-C reveal potential conserved functions for translational regulation in metazoan development. We propose that by binding to BIC-C, upon egg activation GNU brings PNG to its initial targets, translational repressors in RNP granules.

scholarly journals Aurora kinase B inhibits Aurora kinase A to control maternal mRNA translation in mouse oocytes

Development ◽  
2021 ◽  
Author(s):  
Mansour Aboelenain ◽  
Karen Schindler
Keyword(s):  
Mrna Translation ◽  
Aurora Kinase ◽  
Cytoplasmic Polyadenylation ◽  
Aurora Kinase A ◽  
Aurora Kinase B ◽  
Maternal Mrna ◽  
Kinase C ◽  
Maternal Mrnas ◽  
Mrna Polyadenylation ◽  
Kinase A

Mammalian oocytes are transcriptionally quiescent, and meiosis and early embryonic divisions rely on translation of stored maternal mRNAs. Activation of these mRNAs is mediated by polyadenylation. Cytoplasmic polyadenylation binding element 1 (CPEB1) regulates activates mRNA polyadenylation. One message is Aurora kinase C (Aurkc), encoding a protein that regulates chromosome segregation. We previously demonstrated that AURKC levels are upregulated in oocytes lacking Aurora kinase B (AURKB), and this upregulation caused increased aneuploidy rates, a role we investigate here. Using genetic and pharmacologic approaches, we found that AURKB negatively regulates CPEB1-dependent translation of many messages. To determine why translation is increased, we evaluated Aurora kinase A (AURKA), a kinase that activates CPEB1 in other organisms. We find that AURKA activity is increased in Aurkb knockout oocytes and demonstrate that this increase drives the excess translation. Importantly, removal of one copy of Aurka from the Aurkb knockout strain background, reduces aneuploidy rates. This study demonstrates that AURKA is required for CPEB1-dependent translation, and it describes a new AURKB requirement to maintain translation levels through AURKA, a function critical to generating euploid eggs.

scholarly journals Control of PNG kinase, a key regulator of mRNA translation, is coupled to meiosis completion at egg activation

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Masatoshi Hara ◽  
Boryana Petrova ◽  
Terry L Orr-Weaver
Keyword(s):  
Kinase Activity ◽  
Mrna Translation ◽  
Mature Oocyte ◽  
Cyclin B ◽  
Egg Activation ◽  
Regulatory Effect ◽  
Kinase Activation ◽  
Maternal Mrna ◽  
Resistant Form

The oocyte-to-embryo transition involves extensive changes in mRNA translation, regulated in Drosophila by the PNG kinase complex whose activity we show here to be under precise developmental control. Despite presence of the catalytic PNG subunit and the PLU and GNU activating subunits in the mature oocyte, GNU is phosphorylated at Cyclin B/CDK1sites and unable to bind PNG and PLU. In vitro phosphorylation of GNU by CyclinB/CDK1 blocks activation of PNG. Meiotic completion promotes GNU dephosphorylation and PNG kinase activation to regulate translation. The critical regulatory effect of phosphorylation is shown by replacement in the oocyte with a phosphorylation-resistant form of GNU, which promotes PNG-GNU complex formation, elevation of Cyclin B, and meiotic defects consistent with premature PNG activation. After PNG activation GNU is destabilized, thus inactivating PNG. This short-lived burst in kinase activity links development with maternal mRNA translation and ensures irreversibility of the oocyte-to-embryo transition.

Die Expression der Aurora Kinase A korreliert mit dem Wnt-Modulator RACGAP1 im Magenkarzinom

2015 ◽  
Vol 53 (08) ◽  
Author(s):  
J Bornschein ◽  
J Nielitz ◽  
I Drozdov ◽  
M Selgrad ◽  
T Wex ◽  
...  
Keyword(s):  
Aurora Kinase ◽  
Aurora Kinase A ◽  
Kinase A

99mTc-Aminohexylidendiphosphonate and 99mTc-Pyrophos phate in the Scintigraphic Diagnosis of Experimental Cardiomyopathy in Dogs

1987 ◽  
Vol 26 (05) ◽  
pp. 220-223 ◽  
Author(s):  
L. Hadaš ◽  
J. VižĎa ◽  
P. Kafka ◽  
Y. Mazurová ◽  
V. Palicka ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Plasma Levels ◽  
Maximum Accumulation ◽  
Kinase A ◽  
Good Agreement

Experimental cardiomyopathy was provoked in 24 dogs with high intravenous doses of adrenaline and theophylline. These lesions were studied by means of the new agent 99mTc-AHDP and 99mTc-PYP in comparison. Cardiomyopathy could be imaged as early as 4 h after the onset of involvement but not later than 7 days. A maximum accumulation occurred in lesions 24 h old. 99mTc uptake in the myocardium was graded scintigraphically. 99mTc-AHDP was accumulated in the altered’myocardium to a greater extent than 99mTc-PYP. Scintigraphic findings were in good agreement with plasma levels of creatine- kinase. A comparison with histology demonstrated that the maximum accumulation of radiopharmaceuticals occurred at the time when the development of myocardium involvement reached the stage of myocytolysis.

Sign in / Sign up

Export Citation Format

Share Document