Homologue disjunction in mouse oocytes requires proteolysis of securin and cyclin B1

Herbert, Mary; Levasseur, Mark; Homer, Hayden; Yallop, Katie; Murdoch, Alison; McDougall, Alex

doi:10.1038/ncb1062

Cited by 193 publications

(207 citation statements)

References 16 publications

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“…In light of these findings we monitored APC/C activation by expressing securin-EGFP, which is a well-established marker of APC/C activation, 24 in oocytes treated with a low or high NCS concentration ( Fig. S1A and Movie 3).…”

Section: Resultsmentioning

confidence: 99%

DNA damage response during mouse oocyte maturation

Mayer

Baran

Sakakibara³

et al. 2016

Cell Cycle

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Because low levels of DNA double strand breaks (DSBs) appear not to activate the ATM-mediated prophase I checkpoint in full-grown oocytes, there may exist mechanisms to protect chromosome integrity during meiotic maturation. Using live imaging we demonstrate that low levels of DSBs induced by the radiomimetic drug Neocarzinostatin (NCS) increase the incidence of chromosome fragments and lagging chromosomes but do not lead to APC/C activation and anaphase onset delay. The number of DSBs, represented by gH2AX foci, significantly decreases between prophase I and metaphase II in both control and NCS-treated oocytes. Transient treatment with NCS increases >2-fold the number of DSBs in prophase I oocytes, but less than 30% of these oocytes enter anaphase with segregation errors. MRE11, but not ATM, is essential to detect DSBs in prophase I and is involved in H2AX phosphorylation during metaphase I. Inhibiting MRE11 by mirin during meiotic maturation results in anaphase bridges and also increases the number of gH2AX foci in metaphase II. Compromised DNA integrity in mirin-treated oocytes indicates a role for MRE11 in chromosome integrity during meiotic maturation.

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Section: Resultsmentioning

confidence: 99%

DNA damage response during mouse oocyte maturation

Mayer

Baran

Sakakibara³

et al. 2016

Cell Cycle

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“…Difficulties have nonetheless been reported in detecting cohesin by immunofluorescence in vertebrate metaphase chromosomes. In meiosis, separase is also necessary to cleave the Scc1 meiotic homolog and to dissociate cohesin from chromosome arms in yeast (Buonomo et al, 2000), worm (Siomos et al, 2001) and mammals (Herbert et al, 2003), but not in Xenopus (Peter et al, 2001;Taieb et al, 2001). The apparent protection of cohesin in the vicinity of centromeres is intriguing, as it could be conferred by distinct subunit composition of arm and centromeric cohesin complexes, and/or by interaction of the cohesin complex with other centromeric proteins.…”

Section: Introductionmentioning

confidence: 99%

Drosophila cohesins DSA1 and Drad21 persist and colocalize along the centromeric heterochromatin during mitosis

Valdeolmillos

Rufas

Suja

et al. 2004

Biology of the Cell

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Sister chromatid cohesion in eukaryotes is maintained mainly by a conserved multiprotein complex termed cohesin. Drad21 and DSA1 are the Drosophila homologues of the yeast Scc1 and Scc3 cohesin subunits, respectively. We recently identified a Drosophila mitotic cohesin complex composed of Drad21/DSA1/DSMC1/DSMC3. Here we study the contribution of this complex to sister chromatid cohesion using immunofluorescence microscopy to analyze cell cycle chromosomal localization of DSA1 and Drad21 in S2 cells. We observed that DSA1 and Drad21 colocalize during all cell cycle stages in cultured cells. Both proteins remain in the centromere until metaphase, colocalizing at the centromere pairing domain that extends along the entire heterochromatin; the centromeric cohesion protein MEI-S332 is nonetheless reported in a distinct centromere domain. These results provide strong evidence that DSA1 and Drad21 are partners in a cohesin complex involved in the maintenance of sister chromatid arm and centromeric cohesion during mitosis in Drosophila.

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“…However, as mentioned above, cyclin B degradation appears necessary for the transition between two meiotic M-phases in mammalian oocytes. 30,34,35 Despite that the role of the proteasome in this meiotic transition was not questioned in Xenopus laevis oocytes, it was postulated that APC/C is dispensable for this process, suggesting modified targeting of cyclin B to the proteasomes during meiotic M-phase, 36 while in mouse oocytes it is certainly involved. 30,35,37 Thus, different mechanisms could be involved in MPF inactivation during somatic or embryonic mitoses, as well as upon the first or second meiotic division in different species.…”

Section: Introductionmentioning

confidence: 99%

Cyclin B Dissociation from CDK1 Precedes its Degradation Upon MPF Inactivation in Mitotic Extracts of Xenopus laevis Embryos

Chesnel

Bazile²,

Pascal³

et al. 2006

Cell Cycle

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Cyclin B is a regulatory subunit of CDK1 within MPF complex. Degradation of cyclin B via ubiquitin-proteasome pathway seemed to be absolutely required for the M-phase exit. However, inhibition of the proteasome proteolytic activity upon the exit from the meiotic metaphase II-arrest in Xenopus cell-free extract revealed that the proteasome-dependent dissociation of cyclin B from CDK1 is sufficient to inactivate MPF without cyclin B degradation. In this study we analyze whether the same mechanism operates during the exit from mitotic M-phase. We show in Xenopus cell-free extract undergoing the first or the second embryonic mitosis that CDK1 oscillations are not affected by proteasome inhibition with MG132 or ALLN despite effective inhibition of cyclins B degradation. The majority of cyclins B1 and B2 surviving CDK1 inactivation is CDK-free and cyclin B2 becomes resistant to phosphatase λ dephosphorylation. The pool of cyclins B remaining after CDK1 inactivation in the presence of MG132 is mitotically inert, while exogenous or newly synthesized cyclin B activates CDK1. This suggests that cyclins B remain sequestered within the proteasome upon MPF inactivation in the presence of MG132.Comparison of the dynamics of the decline of total and CDK-bound pools of cyclins B1, B2 and B4 upon mitotic exit in absence of protein synthesis reveals that CDK-bound cyclins B diminish clearly faster. Our results thus show that cyclin B dissociation from CDK1 precedes cyclins B degradation upon CDK1 inactivation in mitotic embryo extracts and that proteasome proteolytic activity is dispensable for both activation and inactivation of CDK1 in such extracts.

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Homologue disjunction in mouse oocytes requires proteolysis of securin and cyclin B1

Cited by 193 publications

References 16 publications

DNA damage response during mouse oocyte maturation

DNA damage response during mouse oocyte maturation

Drosophila cohesins DSA1 and Drad21 persist and colocalize along the centromeric heterochromatin during mitosis

Cyclin B Dissociation from CDK1 Precedes its Degradation Upon MPF Inactivation in Mitotic Extracts of Xenopus laevis Embryos

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