Interference with the C-terminal structure of MARF1 causes
defective oocyte meiotic division and female infertility in mice

Cao, Guangyi; Li, Mingzhe; Wang, Hao; Shi, Lei; Su, You-Qiang

doi:10.7555/jbr.32.20170108

Cited by 6 publications

(3 citation statements)

References 24 publications

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“…Chromosome spreading was conducted following a previously published protocol 22 (29353819). To remove the zona pellucida of the oocytes, they were briefly exposed to Tyrode's buffer (pH 2.5) (T1788; Sigma) at 37°C for 30 s. After a 10‐min recovery in fresh medium, the oocytes were fixed on a glass slide using a solution containing 1% PFA and 0.15% Triton X‐100.…”

Section: Methodsmentioning

confidence: 99%

NUSAP1 regulates mouse oocyte meiotic maturation

Yu,

Kong,

Lin

et al. 2023

J of Cellular Biochemistry

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The correct assembly of the spindle apparatus directly regulates the precise separation of chromosomes in mouse oocytes, which is crucial for obtaining high‐quality oocytes capable of successful fertilization. The localization, assembly, migration, and disassembly of the spindle are regulated by a series of spindle‐associated proteins, which exhibit unique expression level variations and specific localization in oocytes. Proteomic analysis revealed that among many representative spindle‐associated proteins, the expression level of nucleolar and spindle‐associated protein 1 (NUSAP1) significantly increased after meiotic resumption, with a magnitude of change higher than that of other proteins. However, the role of NUSAP1 during oocyte meiosis maturation has not been reported. Here, we report that NUSAP1 is distributed within the cell nucleus during the germinal vesicle (GV) oocytes with non‐surrounded nucleolus stage and is not enriched in the nucleus during the GV‐surrounded nucleolus stage. Interestingly, NUSAP1 forms distinct granular aggregates near the spindle poles during the prophase of the first meiotic division (Pro‐MI), metaphase I, and anaphase I/telophase I stages. Nusap1 depletion leads to chromosome misalignment, increased aneuploidy, and abnormal spindle assembly, particularly a decrease in spindle pole width. Correspondingly, RNA‐seq analysis revealed significant suppression of the “establishment of spindle orientation” signaling pathway. Additionally, the attenuation of F‐actin in NUSAP1‐deficient oocytes may affect the asymmetric division process. Gene ontology analysis of NUSAP1 interactomes, identified through mass spectrometry here, revealed significant enrichment for RNA binding. As an RNA‐binding protein, NUSAP1 is likely involved in the regulation of messenger RNA homeostasis by influencing the dynamics of processing (P)‐body components. Overall, our results demonstrate the critical importance of precise regulation of NUSAP1 expression levels and protein localization for maintaining mouse oocyte meiosis.

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Section: Methodsmentioning

confidence: 99%

NUSAP1 regulates mouse oocyte meiotic maturation

Yu,

Kong,

Lin

et al. 2023

J of Cellular Biochemistry

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“…Chromosome spread was conducted as described previously (Guangyi et al, 2018). Zona pellucida was removed by exposing oocytes in Tyrode's buffer (pH2.5) (T1788, sigma) for 30 s at 37°C.…”

Section: Chromosome Spreadingmentioning

confidence: 99%

“…Therefore, abnormal events involving mRNA storage and post‐transcriptional regulation during oocyte meiotic maturation affect the stability of mRNA. Several RNA‐binding proteins have been found to be involved in regulating mRNA homeostasis (Guangyi et al, 2018; Rong et al, 2019; Yao et al, 2018). Deadenylation and oligo‐uridylation regulation are also important mechanisms that regulate mRNA homeostasis (Eckersley‐Maslin et al, 2018; Liu et al, 2018; Morgan et al, 2017; Yu et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

PARP12 regulates mouse oocyte meiotic maturation

Cao

Guo

Chen

et al. 2023

Journal Cellular Physiology

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Poly(ADP-ribosyl)ation (PARylation) is an important post-translational modification of proteins that involves the transfer of ADP-ribose moieties, and plays important roles in many biological processes including DNA repair, gene expression, RNA processing, ribosome biogenesis, and protein translation. Though it is accepted that PARylation is crucial for oocyte maturation, little is known about how Mono(ADP-ribosyl)ation (MARylation) regulates this process. Here, we report that Parp12, a mon(ADP-ribosyl) transferase of poly(ADP-ribosyl) polymerase (PARP) family, was highly expressed at all stages of oocytes during meiotic maturation. At germinal vesicle (GV) stage, PARP12 was mainly distributed in cytoplasm. Interestingly, PARP12 formed granular aggregation near to spindle poles during metaphase I (MI) and metaphase II (MII). PARP12 depletion results in abnormal spindle organization and chromosome misalignment in mouse oocytes. Chromosome aneuploidy frequency in PARP12 knockdown oocytes was significantly increased. Importantly, PARP12 knockdown triggers activation of spindle assembly checkpoint as shown by active BUBR1 in PARP12-KD MI oocytes. Besides, F actin was significantly attenuated in PARP12-KD MI oocytes which may affect the asymmetric division process. Transcriptomic analysis demonstrated that PARP12 depletion disrupts transcriptome homeostasis. Collectively, our results showed that the maternally expressed mono(ADPribosyl) transferases PARP12 was essential for oocyte meiotic maturation in mouse.

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P-bodies directly regulate MARF1-mediated mRNA decay in human cells

Brothers

Fakim

Kajjo

et al. 2022

Nucleic Acids Research

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Processing bodies (P-bodies) are ribonucleoprotein granules that contain mRNAs, RNA-binding proteins and effectors of mRNA turnover. While P-bodies have been reported to contain translationally repressed mRNAs, a causative role for P-bodies in regulating mRNA decay has yet to be established. Enhancer of decapping protein 4 (EDC4) is a core P-body component that interacts with multiple mRNA decay factors, including the mRNA decapping (DCP2) and decay (XRN1) enzymes. EDC4 also associates with the RNA endonuclease MARF1, an interaction that antagonizes the decay of MARF1-targeted mRNAs. How EDC4 interacts with MARF1 and how it represses MARF1 activity is unclear. In this study, we show that human MARF1 and XRN1 interact with EDC4 using analogous conserved short linear motifs in a mutually exclusive manner. While the EDC4–MARF1 interaction is required for EDC4 to inhibit MARF1 activity, our data indicate that the interaction with EDC4 alone is not sufficient. Importantly, we show that P-body architecture plays a critical role in antagonizing MARF1-mediated mRNA decay. Taken together, our study suggests that P-bodies can directly regulate mRNA turnover by sequestering an mRNA decay enzyme and preventing it from interfacing with and degrading targeted mRNAs.

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Interference with the C-terminal structure of MARF1 causes defective oocyte meiotic division and female infertility in mice

Cited by 6 publications

References 24 publications

NUSAP1 regulates mouse oocyte meiotic maturation

NUSAP1 regulates mouse oocyte meiotic maturation

PARP12 regulates mouse oocyte meiotic maturation

P-bodies directly regulate MARF1-mediated mRNA decay in human cells

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