Multiple Requirements of PLK1 during Mouse Oocyte Maturation

Solc, P; Kitajima, Tomoya S.; Yoshida, Shuhei; Brzakova, Adela; Kaido, Masako; Baran, Vladimı́r; Mayer, Alexandra; Samalova, Pavlina; Motlı́k, Jan; Ellenberg, Jan

doi:10.1371/journal.pone.0116783

Cited by 85 publications

(93 citation statements)

References 77 publications

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“…This localization pattern was similar to that of the proteins involved in spindle formation, e.g. MDK28, PLK12930, Septin131, BARC132 and cep5533, all of which have been proved to participate in meiotic spindle assembly. When oocytes were exposed to nocodazole to disassemble microtubules, Kif2a staining partly dispersed into the cytoplasm and reappeared at the inner centromeres.…”

Section: Discussionsupporting

confidence: 73%

Kif2a regulates spindle organization and cell cycle progression in meiotic oocytes

Liang

et al. 2016

Sci Rep

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Kif2a is a member of the Kinesin-13 microtubule depolymerases. Here, we report the expression, subcellular localization and functions of Kif2a during mouse oocyte meiotic maturation. Immunoblotting analysis showed that Kif2a was gradually increased form GV to the M I stages, and then decreased slightly at the M II stage. Confocal microscopy identified that Kif2a localized to the meiotic spindle, especially concentrated at the spindle poles and inner centromeres in metaphase and translocated to the midbody at telophase. Kif2a depletion by siRNA microinjection generated severely defective spindles and misaligned chromosomes, reduced microtubule depolymerization, which led to significant pro-M I/M Iarrest and failure of first polar body (PB1) extrusion. Kif2a-depleted oocytes were also defective in spindle pole localization of γ-tubulin and showed spindle assembly checkpoint (SAC) protein Bub3 at the kinetochores even after 10 hr extended culture. These results demonstrate that Kif2a may act as a microtubule depolymerase, regulating microtubule dynamics, spindle assembly and chromosome congression, and thus cell cycle progression during mouse oocyte meiotic maturation.

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Section: Discussionsupporting

confidence: 73%

Kif2a regulates spindle organization and cell cycle progression in meiotic oocytes

Liang

et al. 2016

Sci Rep

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“…Immunostaining of oocytes with the anti-pS659-BubR1 antibody, which detects Cdk1-dependent phosphorylation of the KARD domain (Elowe et al, 2010;Huang et al, 2008;Kruse et al, 2013), revealed a progressive increase in the amount of phosphorylated BubR1 at the KTs throughout prometaphase and metaphase I ( Figure 4C), whereas the amount of total BubR1 at KTs showed a progressive decrease ( Figure S4A). Moreover, the amount of pT669-BubR1 in the KARD domain, which is mediated by Plk1 (Solc et al, 2015;Suijkerbuijk et al, 2012), also showed a progressive increase ( Figure S4B). Consistent with these results, the overexpression of cyclin B1, which increases Cdk1 activity (Davydenko et al, 2013), increased the amount of pS659-BubR1 ( Figure S4C) and the amount of PP2A-B56 localized to the KTs ( Figure S4D).…”

Section: Pp2a-b56 Gradually Localizes To Kts Throughout Prometaphase mentioning

confidence: 95%

Inherent Instability of Correct Kinetochore-Microtubule Attachments during Meiosis I in Oocytes

Yoshida¹,

Kaido²,

Kitajima³

2015

Developmental Cell

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128

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A model for mitosis suggests that correct kinetochore-microtubule (KT-MT) attachments are stabilized by spatial separation of the attachment sites from Aurora B kinase through sister KT stretching. However, the spatiotemporal regulation of attachment stability during meiosis I (MI) in oocytes remains unclear. Here, we found that in mouse oocytes, Aurora B and C (B/C) are located in close proximity to KT-MT attachment sites after bivalent stretching due to an intrinsic property of the MI chromosomes. The Aurora B/C activity destabilizes correct attachments while allowing a considerable amount of incorrect attachments to form. KT-MT attachments are eventually stabilized through KT dephosphorylation by PP2A-B56 phosphatase, which is progressively recruited to KTs depending on the BubR1 phosphorylation resulting from the timer Cdk1 and independent of bivalent stretching. Thus, oocytes lack a mechanism for coordinating bivalent stretching and KT phosphoregulation during MI, which may explain the high frequency of KT-MT attachment errors.

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“…For example, Polo-like kinase 1 (Plk1) is activated on MTOCs and is required for the localization of other centrosomal proteins to MTOCs. 28 In addition, Bora, known as a binding partner of Aurka, regulates the precise localization of Aurka and Plk1. 29 The protein expression of Bora was significantly reduced, and the levels of Plk1, phosphorylated Tpx2 also showed a decreasing tendency following Bcl2l10 RNAi (Fig.…”

Section: Bcl2l10 Rnai Reduces Mtoc-associated Protein Expressionmentioning

confidence: 99%

Bcl2l10, a new Tpx2 binding partner, is a master regulator of Aurora kinase A in mouse oocytes

Lee

Kim

et al. 2016

Cell Cycle

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Previously, we demonstrated that Bcl-2-like 10 (Bcl2l10) is associated with meiotic spindle assembly and that the gene that is most strongly down-regulated by Bcl2l10 RNAi is targeting protein for Xklp2 (Tpx2). Tpx2 is a well-known cofactor that controls the activity and localization of Aurora kinase A (Aurka) during mitotic spindle assembly. Therefore, this study was conducted (1) to identify the associations among Bcl2l10, Tpx2, and Aurka and (2) to understand how Bcl2l10 regulates meiotic spindle assembly in mouse oocytes. Bcl2l10, Tpx2, and Aurka co-localized on the meiotic spindles, and Bcl2l10 was present in the same complex with Tpx2. Tpx2 and Aurka expression decreased whereas phospho-Aurka increased in Bcl2l10 RNAi-treated oocytes. Counterbalancing changes in the levels of these 2 activators, Tpx2 and phospho-Aurka, resulted in decreased Aurka catalytic activity after Bcl2l10 RNAi treatment. Bcl2l10 RNAi decreased the expression of microtubule organizing center (MTOC)-related proteins, disturbed MTOC formation and disrupted meiotic spindle assembly. Our data demonstrate that Bcl2l10 is a binding partner of Tpx2 and a new regulator of the complex controlling the organization of microtubules and MTOC biogenesis in meiotic spindle assembly. The discovery of Bcl2l10 as a new effector of Aurka suggests that Bcl2l10 may have diverse functions in mitotic cells.

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Multiple Requirements of PLK1 during Mouse Oocyte Maturation

Cited by 85 publications

References 77 publications

Kif2a regulates spindle organization and cell cycle progression in meiotic oocytes

Kif2a regulates spindle organization and cell cycle progression in meiotic oocytes

Inherent Instability of Correct Kinetochore-Microtubule Attachments during Meiosis I in Oocytes

Bcl2l10, a new Tpx2 binding partner, is a master regulator of Aurora kinase A in mouse oocytes

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