Interaction with 14-3-3 Adaptors Regulates the Sorting of hMex-3B RNA-binding Protein to Distinct Classes of RNA Granules

Courchet, Julien; Buchet-Poyau, Karine; Potemski, Auriane; Brès, Aurélie; Jariel-Encontre, Isabelle; Billaud, Marc

doi:10.1074/jbc.m802927200

Cited by 41 publications

(37 citation statements)

References 61 publications

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“…Paralogue of Mex3A, RNA-binding protein, interaction with 14-3-3 prevents association with P-bodies and Ago1 [84,85] hnRNP (heterogenous nuclear RNP) Q RNA-binding protein, co-localizes with P bodies on stress [ …”

Section: Nmd (Nonsense-mediated Mrna Decay)mentioning

confidence: 99%

On track with P-bodies

Kulkarni

Ozgur

Stoecklin

2010

Biochemical Society Transactions

178

160

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P-bodies (processing bodies) are cytoplasmic foci visible by light microscopy in somatic cells of vertebrate and invertebrate origin as well as in yeast, plants and trypanosomes. At the molecular level, P-bodies are dynamic aggregates of specific mRNAs and proteins that serve a dual function: first, they harbour mRNAs that are translationally silenced, and such mRNA can exit again from P-bodies to re-engage in translation. Secondly, P-bodies recruit mRNAs that are targeted for deadenylation and degradation by the decapping/Xrn1 pathway. Whereas certain proteins are core constituents of P-bodies, others involved in recognizing short-lived mRNAs can only be trapped in P-bodies when mRNA decay is attenuated. This reflects the very transient interactions by which many proteins associate with P-bodies. In the present review, we summarize recent findings on the function, assembly and motility of P-bodies. An updated list of proteins and RNAs that localize to P-bodies will help in keeping track of this fast-growing field.

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Section: Nmd (Nonsense-mediated Mrna Decay)mentioning

confidence: 99%

On track with P-bodies

Kulkarni

Ozgur

Stoecklin

2010

Biochemical Society Transactions

178

160

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“…Trophectoderm specification is the first, in which segregation of trophectoderm from the inner cell mass (ICM) represents the formation of the blastocyst [7][8][9]. The outside blastomere cells acquire apicobasal polarity and commit to differentiate into trophectoderm that expresses the caudal-type homeodomain protein Cdx2; the inside cells become ICM, which requires Nanog and Oct4 for further differentiation into epiblast and gives rise to all three germ layers of embryonic tissues [5].…”

Section: Introductionmentioning

confidence: 99%

Rbm46 Regulates Trophectoderm Differentiation by StabilizingCdx2mRNA in Early Mouse Embryos

Wang

Chen²,

Deng³

et al. 2015

Stem Cells and Development

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Blastocyst formation represents the first lineage specification by segregation of the trophectoderm from the inner cell mass in early embryonic development. Transcriptional regulation of Cdx2, which is selectively expressed in and essential for the specification of trophectoderm, has been extensively studied. However, post-transcriptional regulation of Cdx2 remains largely unknown. In this study, we report that RNA-binding protein motif 46 (Rbm46), an RNA-binding motif protein with unknown function, directly binds to and stabilizes Cdx2 mRNA in early mouse embryos. In addition, knockdown of Rbm46 using RNA interference downregulated the majority of trophectoderm markers in mouse embryonic stem cells and blocked the allocation of blastomere cells to the trophectoderm in mouse embryos. Our study revealed a novel mechanism by which Rbm46 regulates trophectoderm specification through stabilizing Cdx2 mRNA in early mouse embryos.

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“…MEX3A and MEX3B proteins localize in P-bodies and stress granules, two structures involved in the storage and turnover of mRNAs (BuchetPoyau et al, 2007;Courchet et al, 2008). MEX3A controls the polarity and stemness of intestinal epithelial cells through the downregulation of the mRNA encoding the CDX2 transcription factor (Pereira et al, 2013b) and, in addition, exhibits a transforming activity when overexpressed in gastric epithelial cells (Jiang et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

The RNA-binding protein Mex3b regulates the spatial organization of the Rap1 pathway

et al. 2014

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The four related mammalian MEX-3 RNA-binding proteins are evolutionarily conserved molecules for which the in vivo functions have not yet been fully characterized. Here, we report that male mice deficient for the gene encoding Mex3b are subfertile. Seminiferous tubules of Mex3b-deficient mice are obstructed as a consequence of the disrupted phagocytic capacity of somatic Sertoli cells. In addition, both the formation and the integrity of the blood-testis barrier are compromised owing to mislocalization of N-cadherin and connexin 43 at the surface of Sertoli cells. We further establish that Mex3b acts to regulate the cortical level of activated Rap1, a small G protein controlling phagocytosis and cell-cell interaction, through the activation and transport of Rap1GAP. The active form of Rap1 (Rap1-GTP) is abnormally increased at the membrane cortex and chemically restoring Rap1-GTP to physiological levels rescues the phagocytic and adhesion abilities of Sertoli cells. Overall, these findings implicate Mex3b in the spatial organization of the Rap1 pathway that orchestrates Sertoli cell functions.

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Interaction with 14-3-3 Adaptors Regulates the Sorting of hMex-3B RNA-binding Protein to Distinct Classes of RNA Granules

Cited by 41 publications

References 61 publications

On track with P-bodies

On track with P-bodies

Rbm46 Regulates Trophectoderm Differentiation by StabilizingCdx2mRNA in Early Mouse Embryos

The RNA-binding protein Mex3b regulates the spatial organization of the Rap1 pathway

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