Inhibition of
            <i>Xenopus</i>
            oocyte meiotic maturation by catalytically inactive protein kinase A

Schmitt, Anja; Nebreda, Ángel R.

doi:10.1073/pnas.022056399

Cited by 64 publications

(73 citation statements)

References 44 publications

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“…More recently, it has been found that injection of catalytically inactive PKA can also block progesterone-and Mosinduced GVBD and partially reduces cyclin B-induced GVBD. By contrast, inactive PKA is completely unable to block Cdc25-induced GVBD (Daar et al, 1993;Matten et al, 1994;Schmitt and Nebreda, 2002). Our results, combined with the observation that the kinase activity of PKA is required for inhibiting activation of cyclin B/Cdc2 by Cdc25, suggest that in addition to Cdc25 in Xenopus oocytes (Duckworth et al, 2002) and Wee1B in mouse oocytes (Han et al, 2005), serine 321 of Cdc25B is a potential target site for PKA phosphorylation in mouse oocytes.…”

Section: Discussionmentioning

confidence: 63%

“…The role of the cAMP/PKA signaling pathway in meiotic resumption of oocytes has been observed in numerous reports. High PKA activity suppresses Mos accumulation and inhibits the ability of injected Mos, cyclinB or Cdc25 to induce GVBD, suggesting that PKA inhibits oocyte maturation at several steps (Daar et al, 1993;Schmitt and Nebreda, 2002). More recently, it has been found that injection of catalytically inactive PKA can also block progesterone-and Mosinduced GVBD and partially reduces cyclin B-induced GVBD.…”

Section: Discussionmentioning

confidence: 99%

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Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

Zhang

et al. 2008

Developmental Dynamics

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Protein kinase A (PKA) play a critical role in maintaining the meiotic arrest. However, the steps downstream of PKA remain largely unknown. In this study, we investigated the regulation of meiotic resumption by PKA/Cdc25B pathway in mouse oocytes. Injection of mRNA coding for Cdc25b-S321A had a more potent maturation-inducing ability than Cdc25b-WT. When co-injected with PKA inhibitor, Cdc25B-WT had similar activities with Cdc25B-S321A. Meanwhile, the phosphorylation of Cdc25B-S321 was detected in germinal vesicle (GV) oocytes by Western blotting with a phospho-Ser321-specific antibody and the band disappeared when oocytes reenter into the meiotic cell cycle. Furthermore, Cdc25B-WT translocated to the nucleus shortly before GV breakdown (GVBD), whereas phosphorylated Cdc25B-S321 expressed exclusively in the cytoplasm and the signal could not be detected in GVBD oocytes. Taken together, these data indicate that Cdc25B-Serine321 is the potential PKA target and Cdc25B subcellular localization determines its function during the process of maintaining GV arrest in mouse oocytes. Developmental Dynamics 237: 3777-3786, 2008.

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Section: Discussionmentioning

confidence: 63%

Section: Discussionmentioning

confidence: 99%

Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

Zhang

et al. 2008

Developmental Dynamics

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“…It has long been known that PKA activity is required to maintain oocytes of all species tested in their natural G 2 arrest and that a drop in PKA activity is required for the G 2 /meiosis I transition (O'Connor and Smith, 1976;Maller and Krebs, 1977;Speaker and Butcher, 1977;Maller et al, 1979;Mulner et al, 1979;Finidori-Lepicard et al, 1981;Huchon et al, 1981;Sadler and Maller, 1981;Masui, 1985). Phosphorylation of cdc25C Ser287 by PKA has recently been shown to be required to maintain the G 2 arrest (Duckworth et al, 2002;Schmitt and Nebreda, 2002). In the early embryonic cell cycles, PKA activity has been reported to oscillate, being high in mitosis and low in interphase, and high PKA activity blocks entry into mitosis (Grieco et al, 1994(Grieco et al, , 1996.…”

Section: Wee1 and Cdc25 Phosphorylationmentioning

confidence: 99%

“…C-TAK1, identified as a human Ser216 phosphorylating activity from mammalian somatic cells, was the first to be described (Ogg et al, 1994;Peng et al, 1998). Protein kinase A (PKA), a well-known inhibitor of the G 2 /meiosis I transition, helps to maintain Xenopus oocytes in their natural G 2 arrest through phosphorylation of cdc25C on Ser287 (Duckworth et al, 2002;Schmitt and Nebreda, 2002). In fertilized Xenopus eggs, calmodulin-dependent protein kinase II (CaMKII) seems to be responsible for the majority of Ser287 phosphorylation during interphase of the first mitotic cell cycle (Hutchins et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Changes in Regulatory Phosphorylation of Cdc25C Ser287 and Wee1 Ser549 during Normal Cell Cycle Progression and Checkpoint Arrests

Stanford

Ruderman

2005

MBoC

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Entry into mitosis is catalyzed by cdc2 kinase. Previous work identified the cdc2-activating phosphatase cdc25C and the cdc2-inhibitory kinase wee1 as targets of the incomplete replication-induced kinase Chk1. Further work led to the model that checkpoint kinases block mitotic entry by inhibiting cdc25C through phosphorylation on Ser287 and activating wee1 through phosphorylation on Ser549. However, almost all conclusions underlying this idea were drawn from work using recombinant proteins. Here, we report that in the early Xenopus egg cell cycles, phosphorylation of endogenous cdc25C Ser287 is normally high during interphase and shows no obvious increase after checkpoint activation. By contrast, endogenous wee1 Ser549 phosphorylation is low during interphase and increases after activation of either the DNA damage or replication checkpoints; this is accompanied by a slight increase in wee1 kinase activity. Blocking mitotic entry by adding the catalytic subunit of PKA also results in increased wee1 Ser549 phosphorylation and maintenance of cdc25C Ser287 phosphorylation. These results argue that in response to checkpoint activation, endogenous wee1 is indeed a critical responder that functions by repressing the cdc2-cdc25C positive feedback loop. Surprisingly, endogenous wee1 Ser549 phosphorylation is highest during mitosis just after the peak of cdc2 activity. Treatments that block inactivation of cdc2 result in further increases in wee1 Ser549 phosphorylation, suggesting a previously unsuspected role for wee1 in mitosis. INTRODUCTIONEntry into mitosis is initiated by activation of cyclin B/cdc2. Preformed complexes of cyclin B/cdc2 accumulate during interphase, but their activity is repressed by inhibitory phosphorylations on cdc2 at Tyr15 (catalyzed by wee1 and myt1) and Thr14 (catalyzed by myt1). These phosphorylations are removed by the phosphatase cdc25C (reviewed in Berry and Gould, 1996;Lew and Kornbluth, 1996). Early work led to the conclusion that cdc2 and cdc25C activities both increase rapidly during the G 2 /M transition as the result of positive feedback loops between cyclin B/cdc2 and cdc25C, ultimately leading to the full activation of both cdc25C and cyclin B/cdc2 (Izumi et al., 1992;Hoffmann et al., 1993;Izumi and Maller, 1993;Strausfeld et al., 1994). The mechanisms that trigger this abrupt activation are still not well understood (Margolis and Kornbluth, 2004;Perdiguero and Nebreda, 2004).Over the past decade, there has been a large increase in the molecular understanding of how checkpoint pathways become activated, and how they affect the basic cell cycle regulatory machinery. Genetic and biochemical approaches have identified sensors that detect incompletely replicated or damaged DNA and that stimulate signal transduction pathways that lead to activation of the kinases Chk1 and Chk2/Cds1 (reviewed in Sancar et al., 2004). Both Chk1 and Chk2 can phosphorylate cdc25C on Ser287 (human Ser216), which creates a binding site for 14-3-3 proteins; this is thought to inhibit cdc25C activation and thus...

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“…During prophase arrest in oocytes, cyclin B-CDK1 remains inactive due to the maintenance of high levels of cAMP within the oocyte and the subsequent sustained activation of protein kinase A (PKA; Figure 3; Mehlmann et al, 2002;Schmitt and Nebreda, 2002). PKA phosphorylates and inactivates the Cdc25 isoform Cdc25B which is responsible for cyclin B-CDK1 activation in oocytes (Lincoln et al, 2002;Pirino et al, 2009;Oh et al, 2010).…”

Section: Prophase Arrestmentioning

confidence: 99%

The DNA Damage Response in Mammalian Oocytes.

Marangos

2012

Biology of Reproduction

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Inhibition of Xenopus oocyte meiotic maturation by catalytically inactive protein kinase A

Cited by 64 publications

References 44 publications

Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

Changes in Regulatory Phosphorylation of Cdc25C Ser287 and Wee1 Ser549 during Normal Cell Cycle Progression and Checkpoint Arrests

The DNA Damage Response in Mammalian Oocytes.

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