Mouse ZAR1‐like (XM_359149) colocalizes with mRNA processing components and its dominant‐negative mutant caused two‐cell‐stage embryonic arrest

Hu, Jianjun; Wang, Fengchao; Zhu, Xiaoquan; Yuan, Ye; Ding, Mei; Gao, Shaorong

doi:10.1002/dvdy.22170

Cited by 43 publications

(42 citation statements)

References 74 publications

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“…It could be that Zar1 and Zar2 are differentially localized within the oocyte and therefore they do not compete for the same mRNAs. For example both Zar1 and Zar2 (Zar1-like) have been found in P-body-like mRNP complexes [1, 38] suggesting that they are not homogenously distributed in the cytoplasm. Alternatively, because Zar1 and Zar2 expression peaks are at different stages of oogenesis this could indicate that they might have access to different mRNAs at these stages.…”

Section: Discussionmentioning

confidence: 99%

“…Zygote arrest (Zar) family proteins have been implicated in the early mitotic cleavages of the embryo, the maternal to zygote transition and epidermalization of the embryo [1–3]. Zar-family expression is generally confined to the oocyte and early embryo in all species tested, but in some species Zar proteins are also expressed in the testis [3–8].…”

Section: Introductionmentioning

confidence: 99%

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Zar1 represses translation in Xenopus oocytes and binds to the TCS in maternal mRNAs with different characteristics than Zar2

Yamamoto

Cook

Kotter

et al. 2013

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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Maternal mRNAs are translationally regulated during early development. Zar1 and its closely related homolog, Zar2, are both crucial in early development. Xenopus laevis Zygote arrest 2 (Zar2) binds to the Translational Control Sequence (TCS) in maternal mRNAs and regulates translation. The molecular mechanism of Zar1 has not been described. Here we report similarities and differences between Xenopus Zar1 and Zar2. Analysis of Zar sequences in vertebrates revealed two Zar family members with conserved, characteristic amino acid differences in the C-terminal domain. The presence of only two vertebrate Zar proteins was supported by analyzing Zar1 synteny. We propose that the criteria for naming Zar sequences are based on the characteristic amino acids and the chromosomal context. We also propose reclassification of some Zar sequences. We found that Zar1 is expressed throughout oogenesis and is stable during oocyte maturation. The N-terminal domain of Zar1 repressed translation of a reporter construct in immature oocytes. Both Zar1 and Zar2 bound to the TCS in the Wee1 and Mos 3′ UTRs using a zinc finger in the C-terminal domain. However, Zar1 had much higher affinity for RNA than Zar2. To show the functional significance of the conserved amino acid substitutions, these residues in Zar2 were mutated to those found in Zar1. We show that these residues contributed to the different RNA binding characteristics of Zar1 compared to Zar2. Our study shows that Zar proteins have generally similar molecular functions in the translational regulation of maternal mRNAs, but they may have different roles in early development.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Zar1 represses translation in Xenopus oocytes and binds to the TCS in maternal mRNAs with different characteristics than Zar2

Yamamoto

Cook

Kotter

et al. 2013

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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“…Consistent with this, a comparison with mammalian mRBPomes revealed that a fraction of our zebrafish MZT mRBPome (9%) has not been previously detected in other mRNA interactomes. Indeed, it has been shown that the depletion of maternal-effect genes, Zar1 and Zar1l, causes embryonic arrest in early mouse embryos (Wu et al 2003;Hu et al 2010). Moreover, lack of maternal Piwi protein in fly embryos causes developmental defects, such as abnormal chromosome morphology and cell cycle arrest (Mani et al 2014).…”

Section: Discussionmentioning

confidence: 99%

Dynamic RNA–protein interactions underlie the zebrafish maternal-to-zygotic transition

Despic

Dejung

et al. 2017

Genome Res.

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During the maternal-to-zygotic transition (MZT), transcriptionally silent embryos rely on post-transcriptional regulation of maternal mRNAs until zygotic genome activation (ZGA). RNA-binding proteins (RBPs) are important regulators of posttranscriptional RNA processing events, yet their identities and functions during developmental transitions in vertebrates remain largely unexplored. Using mRNA interactome capture, we identified 227 RBPs in zebrafish embryos before and during ZGA, hereby named the zebrafish MZT mRNA-bound proteome. This protein constellation consists of many conserved RBPs, some of which are potential stage-specific mRNA interactors that likely reflect the dynamics of RNA-protein interactions during MZT. The enrichment of numerous splicing factors like hnRNP proteins before ZGA was surprising, because maternal mRNAs were found to be fully spliced. To address potentially unique roles of these RBPs in embryogenesis, we focused on Hnrnpa1. iCLIP and subsequent mRNA reporter assays revealed a function for Hnrnpa1 in the regulation of poly(A) tail length and translation of maternal mRNAs through sequence-specific association with 3 ′ UTRs before ZGA. Comparison of iCLIP data from two developmental stages revealed that Hnrnpa1 dissociates from maternal mRNAs at ZGA and instead regulates the nuclear processing of pri-mir-430 transcripts, which we validated experimentally. The shift from cytoplasmic to nuclear RNA targets was accompanied by a dramatic translocation of Hnrnpa1 and other pre-mRNA splicing factors to the nucleus in a transcription-dependent manner. Thus, our study identifies global changes in RNAprotein interactions during vertebrate MZT and shows that Hnrnpa1 RNA-binding activities are spatially and temporally coordinated to regulate RNA metabolism during early development.

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“…In contrast, most factors involved in mRNA translation (e.g., eIF4G and ribosome subunits) are normally absent from P-bodies (Kedersha et al 2005). The functions of some P-body components (e.g., ZAR1l) are unknown (Hu et al 2010). A recent cell-based siRNA screen identified proteins involved in O-linked N-acetylglucosamine (O-GlcNAc) modifications as being important for stressgranule and/or P-body formation, suggesting an important role for post-translational modifications in cytoplasmic granule formation (Ohn et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Unraveling regulation and new components of human P-bodies through a protein interaction framework and experimental validation

Zheng

Chen²,

Shyu³

2011

RNA

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The cellular factors involved in mRNA degradation and translation repression can aggregate into cytoplasmic domains known as GW bodies or mRNA processing bodies (P-bodies). However, current understanding of P-bodies, especially the regulatory aspect, remains relatively fragmentary. To provide a framework for studying the mechanisms and regulation of P-body formation, maintenance, and disassembly, we compiled a list of P-body proteins found in various species and further grouped both reported and predicted human P-body proteins according to their functions. By analyzing protein-protein interactions of human P-body components, we found that many P-body proteins form complex interaction networks with each other and with other cellular proteins that are not recognized as P-body components. The observation suggests that these other cellular proteins may play important roles in regulating P-body dynamics and functions. We further used siRNA-mediated gene knockdown and immunofluorescence microscopy to demonstrate the validity of our in silico analyses. Our combined approach identifies new P-body components and suggests that protein ubiquitination and protein phosphorylation involving 14-3-3 proteins may play critical roles for post-translational modifications of P-body components in regulating P-body dynamics. Our analyses provide not only a global view of human P-body components and their physical interactions but also a wealth of hypotheses to help guide future research on the regulation and function of human P-bodies.

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Mouse ZAR1‐like (XM_359149) colocalizes with mRNA processing components and its dominant‐negative mutant caused two‐cell‐stage embryonic arrest

Cited by 43 publications

References 74 publications

Zar1 represses translation in Xenopus oocytes and binds to the TCS in maternal mRNAs with different characteristics than Zar2

Zar1 represses translation in Xenopus oocytes and binds to the TCS in maternal mRNAs with different characteristics than Zar2

Dynamic RNA–protein interactions underlie the zebrafish maternal-to-zygotic transition

Unraveling regulation and new components of human P-bodies through a protein interaction framework and experimental validation

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