Rab23/Kif17 regulate meiotic progression in oocytes by modulating tubulin acetylation and actin dynamics

Wang, Honghui; Tang, Feng; Pan, Meng-Hao; Wan, Xiang; Li, Xiaohan; Sun, Shao‐Chen

doi:10.1242/dev.171280

Cited by 20 publications

(15 citation statements)

References 46 publications

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“…Researchers identified four kinds of mutations of PANX1 by whole-exome sequencing and observed that mutant GLY1 (one glycosylation form of PANX1) caused oocyte death because of aberrant channel activation ( Sang et al, 2019 ). Other studies showed that acetylation was involved in regulating meiotic progression and maternal-to-zygotic transition ( Wang H. et al, 2019 ; Wang H.H. et al, 2019 ; Zhang et al, 2019 ).…”

Section: Discussionmentioning

confidence: 99%

Post-Translational Modifications in Oocyte Maturation and Embryo Development

Yang

2021

Front. Cell Dev. Biol.

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Mammalian oocyte maturation and embryo development are unique biological processes regulated by various modifications. Since de novo mRNA transcription is absent during oocyte meiosis, protein-level regulation, especially post-translational modification (PTM), is crucial. It is known that PTM plays key roles in diverse cellular events such as DNA damage response, chromosome condensation, and cytoskeletal organization during oocyte maturation and embryo development. However, most previous reviews on PTM in oocytes and embryos have only focused on studies of Xenopus laevis or Caenorhabditis elegans eggs. In this review, we will discuss the latest discoveries regarding PTM in mammalian oocytes maturation and embryo development, focusing on phosphorylation, ubiquitination, SUMOylation and Poly(ADP-ribosyl)ation (PARylation). Phosphorylation functions in chromosome condensation and spindle alignment by regulating histone H3, mitogen-activated protein kinases, and some other pathways during mammalian oocyte maturation. Ubiquitination is a three-step enzymatic cascade that facilitates the degradation of proteins, and numerous E3 ubiquitin ligases are involved in modifying substrates and thus regulating oocyte maturation, oocyte-sperm binding, and early embryo development. Through the reversible addition and removal of SUMO (small ubiquitin-related modifier) on lysine residues, SUMOylation affects the cell cycle and DNA damage response in oocytes. As an emerging PTM, PARlation has been shown to not only participate in DNA damage repair, but also mediate asymmetric division of oocyte meiosis. Each of these PTMs and external environments is versatile and contributes to distinct phases during oocyte maturation and embryo development.

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Section: Discussionmentioning

confidence: 99%

Post-Translational Modifications in Oocyte Maturation and Embryo Development

Yang

2021

Front. Cell Dev. Biol.

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“…Inhibition of different histone deacetylases such as HDAC3, HDAC6, and HDAC11 all could cause spindle defects in oocytes [46][47][48]. Besides, kinesins such as Kif11, Kif17, and Kif18 are shown to affect spindle organization through their effects on microtubule acetylation level during mouse oocyte maturation [49][50][51]. Our results reveal that PRC1 KD resulted in increased acetylation of microtubules in mouse oocytes, while the supplementation of PRC1 mRNA could reduce tubulin acetylation to the normal level, which further confirmed the role of PRC1 in formation of the spindle midzone in mouse oocytes.…”

Section: Discussionmentioning

confidence: 99%

PRC1 is a critical regulator for anaphase spindle midzone assembly and cytokinesis in mouse oocyte meiosis

Pan

et al. 2020

The FEBS Journal

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Protein regulator of cytokinesis 1 (PRC1) is a microtubule bundling protein that is involved in the regulation of the central spindle bundle and spindle orientation during mitosis. However, the functions of PRC1 during meiosis have rarely been studied. In this study, we explored the roles of PRC1 during meiosis using an oocyte model. Our results found that PRC1 was expressed at all stages of mouse oocyte meiosis, and PRC1 accumulated in the midzone/midbody during anaphase/telophase I. Moreover, depleting PRC1 caused defects in polar body extrusion during mouse oocyte maturation. Further analysis found that PRC1 knockdown did not affect meiotic spindle formation or chromosome segregation; however, deleting PRC1 prevented formation of the midzone and midbody at the anaphase/telophase stage of meiosis I, which caused cytokinesis defects and further induced the formation of two spindles in the oocytes. PRC1 knockdown increased the level of tubulin acetylation, indicating that microtubule stability was affected. Furthermore, KIF4A and PRC1 showed similar localization in the midzone/midbody of oocytes at anaphase/telophase I, while the depletion of KIF4A affected the expression and localization of PRC1. The PRC1 mRNA injection rescued the defects caused by PRC1 knockdown in oocytes. In summary, our results suggest that PRC1 is critical for midzone/midbody formation and cytokinesis under regulation of KIF4A in mouse oocytes.

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“…We propose that the recruitment of specific kinesins by MTOCs could be a mechanism for controlling the recruitment of tubulin modifiers. Indeed, recent data in mammalian cells indicate that kinesins control at least some microtubule modifications such as acetylation (Tang et al, 2018; Wang et al, 2019). In addition, microtubule longevity is a prerequisite for the acquisition of many tubulin modifications (Roll-Mecak, 2019).…”

Section: Discussionmentioning

confidence: 99%

Remote control of microtubule plus-end dynamics and function from the minus-end

Chen

Widmer

Stangier

et al. 2019

eLife

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In eukaryotes, the organization and function of the microtubule cytoskeleton depend on the allocation of different roles to individual microtubules. For example, many asymmetrically dividing cells differentially specify microtubule behavior at old and new centrosomes. Here we show that yeast spindle pole bodies (SPBs, yeast centrosomes) differentially control the plus-end dynamics and cargoes of their astral microtubules, remotely from the minus-end. The old SPB recruits the kinesin motor protein Kip2, which then translocates to the plus-end of the emanating microtubules, promotes their extension and delivers dynein into the bud. Kip2 recruitment at the SPB depends on Bub2 and Bfa1, and phosphorylation of cytoplasmic Kip2 prevents random lattice binding. Releasing Kip2 of its control by SPBs equalizes its distribution, the length of microtubules and dynein distribution between the mother cell and its bud. These observations reveal that microtubule organizing centers use minus to plus-end directed remote control to individualize microtubule function.

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Rab23/Kif17 regulate meiotic progression in oocytes by modulating tubulin acetylation and actin dynamics

Cited by 20 publications

References 46 publications

Post-Translational Modifications in Oocyte Maturation and Embryo Development

Post-Translational Modifications in Oocyte Maturation and Embryo Development

PRC1 is a critical regulator for anaphase spindle midzone assembly and cytokinesis in mouse oocyte meiosis

Remote control of microtubule plus-end dynamics and function from the minus-end

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