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Msi1 assists CPEB1-driven polyadenylation [CPEB1 & Msi1 RIP replicate]

ABSTRACT: The translational reactivation of maternal mRNAs encoding the drivers of vertebrate meiosis is accomplished mainly by cytoplasmic polyadenylation. The Cytoplasmic Polyadenylation Elements (CPEs) present in the 3’ UTR of these transcripts, together with their cognate CPE-binding proteins (CPEBs), define a combinatorial code that determines the timing and extent of translational activation upon meiosis resumption. In addition, the RNA-binding protein Musashi1 (Msi1) regulates the polyadenylation of CPE-containing mRNAs by an as yet undefined CPEB-dependent or -independent mechanism. Here we show that Msi1 alone does not support cytoplasmic polyadenylation, but its binding triggers the remodeling of RNA structure, thereby exposing adjacent CPEs and stimulating polyadenylation. Thus, Msi1 directs the preferential use of specific CPEs, which in turn affects the timing and extent of polyadenylation during meiotic progression. Genome-wide analysis of CPEB1- and Msi-associated mRNAs identified 491 common targets, thus revealing a new layer of CPE-mediated translational control.

ORGANISM(S): Xenopus laevis

PROVIDER: GSE68095 | GEO | 2017/07/17

SECONDARY ACCESSION(S): PRJNA281737

REPOSITORIES: GEO

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Msi1 assists CPEB1-driven polyadenylation [CPEB1 RIP]

Project description:The translational reactivation of maternal mRNAs encoding the drivers of vertebrate meiosis is accomplished mainly by cytoplasmic polyadenylation. The Cytoplasmic Polyadenylation Elements (CPEs) present in the 3’ UTR of these transcripts, together with their cognate CPE-binding proteins (CPEBs), define a combinatorial code that determines the timing and extent of translational activation upon meiosis resumption. In addition, the RNA-binding protein Musashi1 (Msi1) regulates the polyadenylation of CPE-containing mRNAs by an as yet undefined CPEB-dependent or -independent mechanism. Here we show that Msi1 alone does not support cytoplasmic polyadenylation, but its binding triggers the remodeling of RNA structure, thereby exposing adjacent CPEs and stimulating polyadenylation. Thus, Msi1 directs the preferential use of specific CPEs, which in turn affects the timing and extent of polyadenylation during meiotic progression. Genome-wide analysis of CPEB1- and Msi-associated mRNAs identified 491 common targets, thus revealing a new layer of CPE-mediated translational control.

2017-07-17 | GSE68098 | GEO

Msi1 assists CPEB1-driven polyadenylation [Msi1 RIP]

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Msi1 assists CPEB1-driven polyadenylation

Project description:Msi1 assists CPEB1-driven polyadenylation

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Expression data from Neuro2a cells treated with siRNA targeting to Cpeb1 mRNA.

Project description:Cytoplasmic polyadenylation element binding protein 1 (CPEB1) regulates polyadenylation and subsequent translation of CPE-containing mRNAs, which contributes to various physiological and pathological phenomena. To clarify changes in gene expression profiles caused by dysregulation of CPEB1 expression, we performed microarray analyses and revealed that reduced CPEB1 expression altered the expression levels of numerous genes. These findings indicate that accurate post-transcriptional regulation of CPEB1 expression contributes to the maintenance of global gene expression partially through modulating lncRNA expression.

2021-03-31 | GSE147604 | GEO

Comparative analyses of vertebrate CPEB-family of proteins define two sub-families with distinct, but coordinated, functions in post-transcriptional regulation of gene expression

Project description:Background: The vertebrate CPEB-family of RNA-binding proteins promote translational repression or activation of their target mRNAs, which harbor cytoplasmic polyadenylation elements (CPEs) in their 3’ UTRs, through cytoplasmic changes in their poly(A) tail lengths. However, their regulation(s) and mechanism(s) of action have not been systematically addressed as a family. Results: Here we perform a comparative analysis of the four vertebrate CPEBs in their regulation by phosphorylation, supramolecular assemblies’ composition and properties and in their mRNA targets. Conclusions: We show that although all four CPEBs are able to recruit CCR4-NOT deadenylation complex when not phosphorylated, their mechanisms of action determine two subfamilies with distinct, but coordinated, regulation by phosphorylation and target specificity. Thus, CPEB1 forms ribonucleoprotein complexes that are remodeled upon a single phosphorylation event, by AurkA, and are associated with mRNAs containing canonical CPEs. On the other hand, CPEB2-4 are regulated by multiple proline-directed phosphorylations that control their liquid-liquid phase-separation. CPEB2-4 mRNA-targets include CPEB1-bound transcripts, with canonical CPEs, but also a specific subset of mRNAs with non-canonical CPEs. In turn, CPEB2-4 coacervates display compositional, morphological and dynamic differences. Altogether, these results show how, globally, the CPEB family of proteins is able to integrate cellular cues to generate a finetuned adaptive response in gene expression regulation.

2022-10-05 | PXD030419 | Pride

Comparative analyses of vertebrate CPEB-family of proteins define two sub-families with distinct, but coordinated, functions in post-transcriptional regulation of gene expressionComparative analyses of vertebrate CPEB-family of proteins define two sub-families with distinct, but coordinated, functions in post-transcriptional regulation of gene expression

2022-10-05 | PXD030480 | Pride

Comparative analyses of vertebrate CPEB-family of proteins define two sub-families with distinct, but coordinated, functions in post-transcriptional regulation of gene expression

2022-10-05 | PXD033349 | Pride

RIP-Chip analysis of Musashi (Msi1)

Project description:RIP-Chip analysis of Msi1 and identification of preferentially associated mRNAs. Keywords: RIP-Chip

2008-07-19 | GSE12171 | GEO

CPEB1-dependent disruption of the mRNA translation program in oocytes during maternal aging

Project description:The molecular causes of deteriorating oocyte quality during aging are poorly defined. Since oocyte developmental competence relies on post-transcriptional regulations, we tested whether defective mRNA translation contributes to this decline in quality. Disruption in ribosome loading on maternal transcripts is present in old oocytes. Using a candidate approach, we detect altered translation of 3’-UTR-reporters and altered poly(A) length of the endogenous mRNAs. mRNA polyadenylation depends on the cytoplasmic polyadenylation binding protein 1 (CPEB1). Cpeb1 mRNA translation and protein levels are decreased in old oocytes. This decrease causes de-repression of Ccnb1 translation in quiescent oocytes, premature CDK1 activation, and accelerated reentry into meiosis. De-repression of Ccnb1 is corrected by Cpeb1 mRNA injection in old oocytes. Oocyte-specific Cpeb1 haploinsufficiency in young oocytes recapitulates all the translation phenotypes of old oocytes. These findings demonstrate that a dysfunction in the oocyte translation program is associated with the decline in oocyte quality during aging.

2023-01-11 | GSE222638 | GEO

CPEB1 or CPEB1 (T171A, S177A) interacting proteome analysis on C2C12 cells

Project description:CPEB1 regulates cellular function by post-transcriptionally controlling its targeted transcripts' translation. After bound to CPEs, CPEB1 recruits cytoplasmic poly (A) polymerase GLD2 to elongate the poly (A) tail for the maintenance of mRNA stability. The stability of mRNA is positively correlated with translational output. It is unexamined whether CPEB1 interacts with translation machinery to regulation translation. Previous reports demonstrate that phosphorylation is required for its regulation on translation. However, it is not well understood whether phosphorylation is essential for CPEB1 interaction with translation machinery or not. Here, we performed mass spectrometry on C2 cells transfected with CPEB1-mVenus or CPEB1 (T171A, S177A)-mVenus after IgG or mVenus antibody immunoprecipitation. After analysis, we identify CPEB1 interacting proteins and the phosphorylation dependent interacting proteins such as ribosomal proteins. Thus, our data suggest that CPEB1 regulate translation by interacting with translation machinery in a phosphorylation dependent manner.

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