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Loss of LSM14b affects the meiosis process of mouse oocytes

ABSTRACT: Loss of LSM14b affects the meiosis process of mouse oocytes

PROVIDER: PRJNA814995 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18299865_1.fastq.gz	Fastqsanger.gz
	SRR18299865_2.fastq.gz	Fastqsanger.gz
	SRR18299866_1.fastq.gz	Fastqsanger.gz
	SRR18299866_2.fastq.gz	Fastqsanger.gz
	SRR18299867_1.fastq.gz	Fastqsanger.gz

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Loss of LSM14b affects the meiosis process of mouse oocytes

Project description:RNA-Seq can comprehensively and quickly obtain almost all transcripts and information of specific cells in rustic states.Here,we compared up-regulated genes in GV and MII oocytes from LSM14b deficient mice and wild-type mice by RNA-Seq,highlighting the important role of LSM14b in meiosis of mouse oocytes.

2023-12-01 | GSE198414 | GEO

Comparing the Transcriptomes of WT oocytes with Lsm14b KO oocytes by RNA-Seq Analysis

Project description:The success of human reproduction relies on high quality oocytes. Oocyte quality is manifested by the competence to complete meiosis, to be fertilized, and to support embryonic development. This meiotic and developmental competence is gradually established during the course of oocyte and follicle development, and is determined in large part by the autonomous gene expression program intrinsic to the oocyte. In order to explore the regulatory role of LSM14B in oocyte, we analyzed the effect of Lsm14b KO on gene expression in GV-stage fully-grown oocytes (FGOs) in mice by comparing the corresponding transcriptomes via RNA-Seq Analysis.

2023-09-08 | GSE204773 | GEO

Mus_Oocyte_LC-MS/MS-mRBPome capture of oocytes identifies the RNA-binding protein LSM14B, an essential regulator of meiosis in mouse oocytes

Project description:A quantitative mass-spectrometry-based proteome profiles of oocytes in WT and Lsm14b KO mouse

2023-07-20 | PXD034070 | Pride

LSM14B is essential for oocyte meiotic maturation by regulating maternal mRNA storage and clearance

Project description:Fully grown oocytes remain transcriptionally quiescent, yet many maternal mRNAs are synthesized and retained in growing oocytes. We now know that maternal mRNAs are stored in a structure called the mitochondria associated ribonucleoprotein domain (MARDO). But the components and functions of MARDO remain elusive. Here, we found that LSM14B knockout prevents the proper storage and timely clearance of mRNAs (including Cyclin B1, Btg4, and other mRNAs that are translationally activated during meiotic maturation), specifically by disrupting MARDO assembly during oocyte growth and meiotic maturation. With decreased levels of storage and clearance, the LSM14B knockout oocytes failed to enter meiosis II, ultimately resulting in female infertility. Our results demonstrate the function of LSM14B in MARDO assembly, couple the MARDO with mRNA clearance and oocyte meiotic maturation.

2023-10-15 | GSE231648 | GEO

Identifying the Translatome of WT and Lsm14b KO GV-Stage Oocytes in mice via Scarce Sample Polysome Profiling (SSP-profiling)

Project description:RNA-binding proteins (RBPs) have essential functions during oocyte development.In order to explore the regulatory role of RNA-binding protein LSM14B in oocyte, we Identified the translatome of WT and Lsm14b KO GV-Stage Oocytes in mice via Scarce Sample Polysome Profiling (SSP-profiling).

2023-09-08 | GSE206270 | GEO

LSM14B is essential for oocyte meiotic maturation by regulating maternal mRNA storage and clearance

2023-10-17 | PXD042761 | Pride

Comparing the Transcriptomes of WT oocytes with Lsm14b KO oocytes by RNA-Seq Analysis

Project description:Comparing the Transcriptomes of WT oocytes with Lsm14b KO oocytes by RNA-Seq Analysis

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Mouse，oocyte ，LC-MS/MS-mRBPome capture of oocytes identifies the RNA-binding protein LSM14B,an essential regulator of meiosis in mouse oocytes

Project description:proteins from immunoprecipitation (IP) of LSM14B indentified by mass spectrometry

2023-07-20 | PXD034185 | Pride

Maternal administration of acetaminophen affects meiosis through its metabolite NAPQI targeting SIRT7 in fetal oocytes

Project description:Maternal administration of acetaminophen affects meiosis through its metabolite NAPQI targeting SIRT7 in fetal oocytes

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Selective dephosphorylation by PP2A-B55 directs the meiosis I - meiosis II transition in oocytes

Project description:Meiosis is a specialized cell cycle that requires sequential changes to the cell division machinery to facilitate changing functions. To define the mechanisms that enable the oocyte-to-embryo transition, we performed time-course proteomics in sea star oocytes from prophase I through the first embryonic cleavage. Although protein levels are broadly stable, dynamic waves of phosphorylation underlie each meiotic stage. We find that the phosphatase PP2A-B55 is reactivated at the Meiosis I/II transition resulting in the preferential dephosphorylation of threonine residues. Selective dephosphorylation is critical for directing the MI / MII transition as altering PP2A-B55 substrate preferences disrupts key cell cycle events after meiosis I. In addition, threonine to serine substitution of a conserved phosphorylation site in the substrate INCENP prevents its relocalization at anaphase I. Thus, through its inherent phospho-threonine preference, PP2A-B55 imposes specific phosphoregulated behaviors that distinguish the two meiotic divisions.

2020-08-14 | MSV000085949 | MassIVE

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