A clean start: degradation of maternal proteins at the oocyte-to-embryo transition

DeRenzo, Cynthia; Seydoux, Géraldine

doi:10.1016/j.tcb.2004.07.005

Cited by 93 publications

(72 citation statements)

References 57 publications

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“…This is consistent with the ubiquitination of MVP in the metaphase-II-arrested ova and with its accelerated degradation after fertilization. This MVP proteolysis could be a result of targeted protein turnover in the fertilized ova, or a consequence of developmentally programmed degradation of stored maternal proteins during oocyte-to-embryo transition, as proposed recently for other ubiquitinated maternal proteins in the invertebrate zygote (DeRenzo & Seydoux 2004). The accumulation pattern of MVP in the porcine zygotes treated with inhibitors of proteasomal protein degradation is reminiscent of MVP accumulation found in poor-quality human oocytes, and in the abnormal porcine zygotes and embryos generated by IVF and SCNT.…”

Section: Discussionmentioning

confidence: 76%

Expression and proteasomal degradation of the major vault protein (MVP) in mammalian oocytes and zygotes

Šutovský¹,

Manandhar²,

Laurinčík³

et al. 2005

Reproduction

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Major vault protein (MVP), also called lung resistance-related protein is a ribonucleoprotein comprising a major part (>70%) of the vault particle. The function of vault particle is not known, although it appears to be involved in multi-drug resistance and cellular signaling. Here we show that MVP is expressed in mammalian, porcine, and human ova and in the porcine preimplantation embryo. MVP was identified by matrix-assisted laser-desorption ionization-time-of-flight (MALDI-TOF) peptide sequencing and Western blotting as a protein accumulating in porcine zygotes cultured in the presence of specific proteasomal inhibitor MG132. MVP also accumulated in poor-quality human oocytes donated by infertile couples and porcine embryos that failed to develop normally after in vitro fertilization or somatic cell nuclear transfer. Normal porcine oocytes and embryos at various stages of preimplantation development showed mostly cytoplasmic labeling, with increased accumulation of vault particles around large cytoplasmic lipid inclusions and membrane vesicles. Occasionally, MVP was associated with the nuclear envelope and nucleolus precursor bodies. Nucleotide sequences with a high degree of homology to human MVP gene sequence were identified in porcine oocyte and endometrial cell cDNA libraries. We interpret these data as the evidence for the expression and ubiquitin-proteasome-dependent turnover of MVP in the mammalian ovum. Similar to carcinoma cells, MVP could fulfill a cell-protecting function during early embryonic development.

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Section: Discussionmentioning

confidence: 76%

Expression and proteasomal degradation of the major vault protein (MVP) in mammalian oocytes and zygotes

Šutovský¹,

Manandhar²,

Laurinčík³

et al. 2005

Reproduction

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“…Second, from the mammalian system we know that paternal mitochondria are selectively tagged (ubiquitinated) during spermatogenesis followed by their degradation by the 26S proteasome when sperm mitochondria enter the egg cytoplasm (Sutovsky et al, 1999). Assuming this mechanism also applies to Drosophila and that the mitochondrial remnants in Drosophila midgut are a rudiment of sperm mitochondrion degradation in the zygote, a distinct window of opportunity presents itself during which such a mechanism could fail: a widespread proteasomal degradation of proteins left from oogenesis occurs in the Drosophila zygote at the onset of embryo development (DeRenzo and Seydoux, 2004). If this process is compromised, then some mitochondria could escape and propagate their DNA.…”

Section: Discussionmentioning

confidence: 99%

Paternal transmission of mitochondrial DNA as an integral part of mitochondrial inheritance in metapopulations of Drosophila simulans

et al. 2012

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Maternal inheritance is one of the hallmarks of animal mitochondrial DNA (mtDNA) and central to its success as a molecular marker. This mode of inheritance and subsequent lack of heterologous recombination allows us to retrace evolutionary relationships unambiguously down the matriline and without the confounding effects of recombinant genetic information. Accumulating evidence of biparental inheritance of mtDNA (paternal leakage), however, challenges our current understanding of how this molecule is inherited. Here, using Drosophila simulans collected from an East African metapopulation exhibiting recurring mitochondrial heteroplasmy, we conducted single fly matings and screened F1 offspring for the presence of paternal mtDNA using allele-specific PCR assays (AS-PCR). In all, 27 out of 4092 offspring were identified as harboring paternal mtDNA, suggesting a frequency of 0.66% paternal leakage in this species. Our findings strongly suggest that recurring mtDNA heteroplasmy as observed in natural populations of Drosophila simulans is most likely caused by repeated paternal leakage. Our findings further suggest that this phenomenon to potentially be an integral part of mtDNA inheritance in these populations and consequently of significance for mtDNA as a molecular marker.

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“…Despite its importance, however, the precise mechanism of CPEB degradation is not known (7,26). In this study, we have elucidated the molecular mechanism of CPEB degradation in Xenopus oocytes, which is summarized in Fig.…”

Section: Discussionmentioning

confidence: 99%

Mechanism of degradation of CPEB during Xenopus oocyte maturation

Setoyama

Yamashita

Sagata

2007

Proc. Natl. Acad. Sci. U.S.A.

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CPEB, a cytoplasmic polyadenylation element-binding protein, plays an important role in translational control of maternal mRNAs in early animal development. During Xenopus oocyte maturation, CPEB undergoes a Cdc2-mediated phosphorylation-and ubiquitindependent degradation that is required for proper entry into meiosis II. However, the precise mechanism of CPEB degradation, including the identity of the responsible E3 ubiquitin ligase, is not known. Here, we show that the SCF ␤-TrCP E3 ubiquitin ligase complex targets CPEB for degradation during Xenopus oocyte maturation. ␤-TrCP, the F-box protein of SCF ␤-TrCP , specifically binds to a sequence 190TSGFSS195 (termed here the TSG motif) of CPEB, thereby targeting CPEB for degradation. ␤-TrCP binding depends on phosphorylation of Thr-190, Ser-191, and Ser-195 in the TSG motif. Among these residues, Ser-191 is phosphorylated by the Polo-like kinase Plx1, which binds CPEB at a specific Thr-125 residue prephosphorylated by Cdc2. Finally, Cdc2-mediated phosphorylation of other multiple Ser residues, previously implicated in CPEB degradation, is required for both Thr-125 phosphorylation and ␤-TrCP binding, presumably causing conformational changes of CPEB. We propose that Cdc2 and Plx1 sequentially phosphorylate CPEB and target it for SCF ␤-TrCP -dependent degradation in Xenopus oocytes. We suggest that many other proteins carrying the TSGlike motif may be targeted by SCF ␤-TrCP .cdc2 ͉ phosphorylation ͉ Plk1/Plx1 ͉ SCF ␤-TrCP ubiquitin ligase ͉ translation

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A clean start: degradation of maternal proteins at the oocyte-to-embryo transition

Cited by 93 publications

References 57 publications

Expression and proteasomal degradation of the major vault protein (MVP) in mammalian oocytes and zygotes

Expression and proteasomal degradation of the major vault protein (MVP) in mammalian oocytes and zygotes

Paternal transmission of mitochondrial DNA as an integral part of mitochondrial inheritance in metapopulations of Drosophila simulans

Mechanism of degradation of CPEB during Xenopus oocyte maturation

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