Calcineurin-dependent Protein Phosphorylation Changes During Egg Activation in Drosophila melanogaster

Zhang, Zijing; Ahmed-Braimah, Yasir H.; Goldberg, Michael L.; Wolfner, Mariana F.

doi:10.1074/mcp.ra118.001076

Cited by 21 publications

(30 citation statements)

References 87 publications

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“…Its autoinhibition is governed by a threonine 286 residue. CaMKII is activated by the binding of Ca 2+ /CaM [41][42][43][44][45][46]. When CaMKII was phosphorylated at Thr286, it activates permanently.…”

Section: Discussionmentioning

confidence: 99%

Involvement of CaMKII in regulating the release of diplotene-arrested mouse oocytes by pAkt1 (Ser473)

Liu

Labbe

et al. 2019

Cell Cycle

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Calcium (Ca2+)/calmodulin-dependent protein kinase II (CaMKII) had been reported to play a role in the process of fertilization. However, the role of CaMKII in the release of diplotene-arrested oocytes is poorly understood. In this study, we explored the potential effect of CaMKII on Akt1 and the relationship among CaMKII, Akt1 and phosphatidylinositol (3,4,5)-trisphosphate (PIP3) during the meiotic resumption of mouse oocytes. We found that inhibition of CaMKII aggravated diplotene arrest. We detected the expression and distribution of pCaMKII (Thr286), pAkt1 (Ser473), Cdc25B and pCdc2 (Tyr15) when oocytes were treated with KN-93, SH-6, LY294002 or PIP3, respectively. Our data showed that down-regulated CaMKII by KN-93 decreased the levels of pAkt1 (Ser473) and rearranged the distribution of pAkt1 (Ser473). Meanwhile, down-regulated pAkt1 (Ser473) by SH-6 also decreased the levels of pCaMKII (Thr286), Cdc25B and pCdc2 (Tyr15) significantly and rearranged the distributions of pCaMKII (Thr286). Furthermore, our data showed that exogenous PIP3 up-regulated GVBD rates significantly and increased the levels of pCaMKII (Thr286) and pAkt1 (Ser473). On the contrary, down-regulation of PIP3 by LY294002 decreased GVBD rates and the levels of pCaMKII (Thr286) and pAkt1 (Ser473), respectively. Our results showed that Akt1 and CaMKII regulated each other, and PIP3 may be involved in these regulations during the release of mouse oocytes from diplotene arrest.

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Section: Discussionmentioning

confidence: 99%

Involvement of CaMKII in regulating the release of diplotene-arrested mouse oocytes by pAkt1 (Ser473)

Liu

Labbe

et al. 2019

Cell Cycle

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“…We undertook a proteomic and phosphoproteomic strategy using oocytes of the sea star Patiria miniata. Prior analyses have revealed proteome-wide changes in animal models including Xenopus, Drosophila, and sea urchins (Guo et al, 2015;Krauchunas et al, 2012;Presler et al, 2017;Zhang et al, 2019). However, the biology of these organisms limits access to a comprehensive series of time points spanning prophase I through the embryonic divisions including the critical meiosis I/II transition.…”

Section: Introductionmentioning

confidence: 99%

Selective dephosphorylation by PP2A-B55 directs the meiosis I - meiosis II transition in oocytes

Swartz

Nguyen

McEwan

et al. 2020

Preprint

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Meiosis is a specialized cell cycle that requires sequential changes to the cell division machinery to facilitate changing functions. To define the mechanisms that enable the oocyte-to-embryo transition, we performed time-course proteomics in sea star oocytes from prophase I through the first embryonic cleavage. Although protein levels are broadly stable, dynamic waves of phosphorylation underlie each meiotic stage. We find that the phosphatase PP2A-B55 is reactivated at the Meiosis I/II transition resulting in the preferential dephosphorylation of threonine residues. Selective dephosphorylation is critical for directing the MI / MII transition as altering PP2A-B55 substrate preferences disrupts key cell cycle events after meiosis I. In addition, threonine to serine substitution of a conserved phosphorylation site in the substrate INCENP prevents its relocalization at anaphase I. Thus, through its inherent phospho-threonine preference, PP2A-B55 rewires the cell division apparatus to direct the MI / MII transition.

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“…This calcium rise, which can result from influx of extracellular calcium and/or the release of calcium from internal stores, leads to dramatic changes in the mature oocyte that prepare it for further development. Many of these changes require the activity of calcium‐dependent kinases and phosphatases (Horner et al, ; Mochida & Hunt, ; Takeo, Hawley, & Aigaki, ; Takeo, Tsuda, Akahori, Matsuo, & Aigaki, ), which alter the phosphoproteome of the egg (Guo et al, ; Krauchunas, Horner, & Wolfner, ; Presler et al, ; Roux, Radeke, Goel, Mushegian, & Foltz, ; Zhang, Ahmed‐Braimah, Goldberg, & Wolfner, ; reviewed in Krauchunas & Wolfner, ).…”

Section: Introductionmentioning

confidence: 99%

“…further development. Many of these changes require the activity of calcium-dependent kinases and phosphatases (Horner et al, 2006;Mochida & Hunt, 2007;Takeo, Hawley, & Aigaki, 2010;Takeo, Tsuda, Akahori, Matsuo, & Aigaki, 2006), which alter the phosphoproteome of the egg (Guo et al, 2015;Krauchunas, Horner, & Wolfner, 2012;Presler et al, 2017;Roux, Radeke, Goel, Mushegian, & Foltz, 2008;Zhang, Ahmed-Braimah, Goldberg, & Wolfner, 2019;reviewed in Krauchunas & Wolfner, 2013).…”

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confidence: 99%

A calcium‐mediated actin redistribution at egg activation in Drosophila

York-Andersen

Wood

et al. 2019

Molecular Reproduction Devel

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Egg activation is the essential process in which mature oocytes gain the competency to proceed into embryonic development. Many events of egg activation are conserved, including an initial rise of intracellular calcium. In some species, such as echinoderms and mammals, changes in the actin cytoskeleton occur around the time of fertilization and egg activation. However, the interplay between calcium and actin during egg activation remains unclear. Here, we use imaging, genetics, pharmacological treatment, and physical manipulation to elucidate the relationship between calcium and actin in living Drosophila eggs. We show that, before egg activation, actin is smoothly distributed between ridges in the cortex of the dehydrated mature oocytes. At the onset of egg activation, we observe actin spreading out as the egg swells though the intake of fluid. We show that a relaxed actin cytoskeleton is required for the intracellular rise of calcium to initiate and propagate. Once the swelling is complete and the calcium wave is traversing the egg, it leads to a reorganization of actin in a wavelike manner. After the calcium wave, the actin cytoskeleton has an even distribution of foci at the cortex. Together, our data show that calcium resets the actin cytoskeleton at egg activation, a model that we propose to be likely conserved in other species.

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Calcineurin-dependent Protein Phosphorylation Changes During Egg Activation in Drosophila melanogaster

Cited by 21 publications

References 87 publications

Involvement of CaMKII in regulating the release of diplotene-arrested mouse oocytes by pAkt1 (Ser473)

Involvement of CaMKII in regulating the release of diplotene-arrested mouse oocytes by pAkt1 (Ser473)

Selective dephosphorylation by PP2A-B55 directs the meiosis I - meiosis II transition in oocytes

A calcium‐mediated actin redistribution at egg activation in Drosophila

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