Differential Regulation of Cdc2 and Cdk2 by RINGO and Cyclins

Karaı̈skou, Anthi; Perez, Laurent; Ferby, Ingvar; Ozon, René; Jessus, Catherine; Nebreda, Ángel R.

doi:10.1074/jbc.m104722200

Cited by 80 publications

(98 citation statements)

References 50 publications

(46 reference statements)

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“…Active Cyclin B-Cdk1, synonymous with maturation promotion factor (MPF), is the catalytic function necessary for the onset of the meiotic divisions [86]. MPF activation is initiated by Ringo and it is supported by Mos and possibly Emi1 [31,[86][87][88][89]. In addition to promoting maturation by activating MPF, Mos is also necessary for the secondary arrest at metaphase II [90], whereas the role of Emi1 in controlling meiotic progression is still under debate [86,[91][92][93].…”

Section: Developmental Control Of the Cell Cycle Via Translational Rementioning

confidence: 99%

Translational regulation of the cell cycle: when, where, how and why?

Kronja

Orr‐Weaver

2011

Phil. Trans. R. Soc. B

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Translational regulation contributes to the control of archetypal and specialized cell cycles, such as the meiotic and early embryonic cycles. Late meiosis and early embryogenesis unfold in the absence of transcription, so they particularly rely on translational repression and activation of stored maternal mRNAs. Here, we present examples of cell cycle regulators that are translationally controlled during different cell cycle and developmental transitions in model organisms ranging from yeast to mouse. Our focus also is on the RNA-binding proteins that affect cell cycle progression by recognizing special features in untranslated regions of mRNAs. Recent research highlights the significance of the cytoplasmic polyadenylation element-binding protein (CPEB). CPEB determines polyadenylation status, and consequently translational efficiency, of its target mRNAs in both transcriptionally active somatic cells as well as in transcriptionally silent mature Xenopus oocytes and early embryos. We discuss the role of CPEB in mediating the translational timing and in some cases spindle-localized translation of critical regulators of Xenopus oogenesis and early embryogenesis. We conclude by outlining potential directions and approaches that may provide further insights into the translational control of the cell cycle.

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Section: Developmental Control Of the Cell Cycle Via Translational Rementioning

confidence: 99%

Translational regulation of the cell cycle: when, where, how and why?

Kronja

Orr‐Weaver

2011

Phil. Trans. R. Soc. B

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“…Mos facilitates MI entry through activation of the ERK-MAPK pathway, which promotes Cdc2 activation by antagonizing its inhibitory kinase, Myt1, and by enhancing the activity of its activating phosphatase, Cdc25 (Sagata et al, 1988;Palmer et al, 1998;Peter et al, 2002). An additional Cdc2 activator, Ringo, has also been implicated in MI entry; this protein both drives maximal Cdc2 activation and renders Cdc2 less susceptible than cyclin-bound Cdc2 to the inhibitory action of Myt1 kinase (Ferby et al, 1999;Karaiskou et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Cdc2 and Mos Regulate Emi2 Stability to Promote the Meiosis I–Meiosis II Transition

Tang

Guo

et al. 2008

MBoC

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The transition of oocytes from meiosis I (MI) to meiosis II (MII) requires partial cyclin B degradation to allow MI exit without S phase entry. Rapid reaccumulation of cyclin B allows direct progression into MII, producing a cytostatic factor (CSF)-arrested egg. It has been reported that dampened translation of the anaphase-promoting complex (APC) inhibitor Emi2 at MI allows partial APC activation and MI exit. We have detected active Emi2 translation at MI and show that Emi2 levels in MI are mainly controlled by regulated degradation. Emi2 degradation in MI depends not on Ca2+/calmodulin-dependent protein kinase II (CaMKII), but on Cdc2-mediated phosphorylation of multiple sites within Emi2. As in MII, this phosphorylation is antagonized by Mos-mediated recruitment of PP2A to Emi2. Higher Cdc2 kinase activity in MI than MII allows sufficient Emi2 phosphorylation to destabilize Emi2 in MI. At MI anaphase, APC-mediated degradation of cyclin B decreases Cdc2 activity, enabling Cdc2-mediated Emi2 phosphorylation to be successfully antagonized by Mos-mediated PP2A recruitment. These data suggest a model of APC autoinhibition mediated by stabilization of Emi2; Emi2 proteins accumulate at MI exit and inhibit APC activity sufficiently to prevent complete degradation of cyclin B, allowing MI exit while preventing interphase before MII entry.

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“…Conversely, these events were blocked or delayed if progesterone-treated oocytes were injected with antisense oligodeoxynucleotides (AS ODN) against RINGO/Spy mRNA (Ferby et al 1999;Lenormand et al 1999). RINGO/Spy binds to and activates cdk1 (and cdk2) as well as associates with p27, the cdk inhibitor, indicating its molecular function in cell cycle regulation (Karaiskou et al 2001;Porter et al 2003;Dinarina et al 2005). RINGO/Spy may associate with free cdk1 in oocytes and eventually trigger MPF activation and maturation.…”

mentioning

confidence: 99%

Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation

Padmanabhan¹,

Richter²

2006

Genes Dev.

125

174

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CPEB is a sequence-specific RNA-binding protein that controls the polyadenylation-induced translation of mos and cyclin B1 mRNAs in maturing Xenopus oocytes. CPEB activity requires not only the phosphorylation of S174, but also the synthesis of a heretofore-unknown upstream effector molecule. We show that the synthesis of RINGO/Spy, an atypical activator of cyclin-dependent kinases (cdks), is necessary for CPEB-directed polyadenylation. Deletion analysis and mRNA reporter assays show that a cis element in the RINGO/Spy 3 UTR is necessary for translational repression in immature (G2-arrested) oocytes. The repression is mediated by 3 UTR Pumilio-Binding Elements (PBEs), and by its binding protein Pumilio 2 (Pum2). Pum2 also interacts with the Xenopus homolog of human Deleted for Azoospermia-like (DAZL) and the embryonic poly(A)-binding protein (ePAB). Following the induction of maturation, Pum2 dissociates not only from RINGO/Spy mRNA, but from XDAZL and ePAB as well; as a consequence, RINGO/Spy mRNA is translated. These results demonstrate that a reversible Pum2 interaction controls RINGO/Spy mRNA translation and, as a result, CPEB-mediated cytoplasmic polyadenylation.

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Differential Regulation of Cdc2 and Cdk2 by RINGO and Cyclins

Cited by 80 publications

References 50 publications

Translational regulation of the cell cycle: when, where, how and why?

Translational regulation of the cell cycle: when, where, how and why?

Cdc2 and Mos Regulate Emi2 Stability to Promote the Meiosis I–Meiosis II Transition

Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB activation

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