Bruno Inhibits the Expression of Mitotic Cyclins during the Prophase I Meiotic Arrest of Drosophila Oocytes

Sugimura, Isamu; Lilly, Mary A.

doi:10.1016/j.devcel.2005.10.018

Cited by 90 publications

(114 citation statements)

References 50 publications

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“…16, we found that the levels of Cyclin A protein are markedly lower during prophase I arrest than in earlier stages (Fig. 1A, stages 1-6 versus stage 10).…”

mentioning

confidence: 71%

“…Although these cells are connected by cytoplasmic bridges, solely the oocyte goes through meiosis, while the nurse cells become polyploid by the endo cycle. Cyclin A protein levels are controlled posttranscriptionally early in oogenesis by deadenylation of the mRNA (15) and during the prophase I arrest by repression of translation by Bruno (16). After oocyte maturation Cyclin A is degraded by metaphase I by targeting by APC/C Cort (10).…”

mentioning

confidence: 99%

“…Although the oocyte is stockpiled with cyclin A mRNA, it is blocked from translation during prophase I arrest by the Bruno translational repressor, shown by Sugimura and Lilly to bind to the 3ЈUTR of the mRNA (16). Failure of this repression leads to loss of the prophase I arrest, and Bruno protein was undetectable at metaphase I (16).…”

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confidence: 99%

See 2 more Smart Citations

Regulation of Cyclin A protein in meiosis and early embryogenesis

Vardy

Pesin

Orr‐Weaver

2009

Proc. Natl. Acad. Sci. U.S.A.

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“…16, we found that the levels of Cyclin A protein are markedly lower during prophase I arrest than in earlier stages (Fig. 1A, stages 1-6 versus stage 10).…”

mentioning

confidence: 71%

mentioning

confidence: 99%

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Regulation of Cyclin A protein in meiosis and early embryogenesis

Vardy

Pesin

Orr‐Weaver

2009

Proc. Natl. Acad. Sci. U.S.A.

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“…In Drosophila, translational repression of Cyclin A is needed to maintain the oocyte arrested in meiosis [29]. Cyclin A accumulation in the oocyte is prevented by the translational repressor Bruno (figure 2c).…”

Section: Developmental Control Of the Cell Cycle Via Translational Rementioning

confidence: 99%

Translational regulation of the cell cycle: when, where, how and why?

Kronja

Orr‐Weaver

2011

Phil. Trans. R. Soc. B

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Translational regulation contributes to the control of archetypal and specialized cell cycles, such as the meiotic and early embryonic cycles. Late meiosis and early embryogenesis unfold in the absence of transcription, so they particularly rely on translational repression and activation of stored maternal mRNAs. Here, we present examples of cell cycle regulators that are translationally controlled during different cell cycle and developmental transitions in model organisms ranging from yeast to mouse. Our focus also is on the RNA-binding proteins that affect cell cycle progression by recognizing special features in untranslated regions of mRNAs. Recent research highlights the significance of the cytoplasmic polyadenylation element-binding protein (CPEB). CPEB determines polyadenylation status, and consequently translational efficiency, of its target mRNAs in both transcriptionally active somatic cells as well as in transcriptionally silent mature Xenopus oocytes and early embryos. We discuss the role of CPEB in mediating the translational timing and in some cases spindle-localized translation of critical regulators of Xenopus oogenesis and early embryogenesis. We conclude by outlining potential directions and approaches that may provide further insights into the translational control of the cell cycle.

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“…Two neuronal nuclei-restricted RNAbinding proteins, UNC-75 and EXC-7, are required for synaptic transmission without affecting neuronal development or synaptogenesis in C. elegans (34). UNC-75 is the C. elegans ortholog of the CELF͞BrunoL family of proteins that control pre-mRNA splicing in mammals (35,36) and mediate translation repression in Drosophila oocytes (37,38). EXC-7 is the C. elegans ELAV (embryonic lethal abnormal vision)͞Hu family protein, a neuron-specific alternative splicing factor in Drosophila (39)(40)(41)(42) and neuron-specific RNA-processing regulator in mammals (43)(44)(45).…”

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confidence: 99%

The C2H2 zinc-finger protein SYD-9 is a putative posttranscriptional regulator for synaptic transmission

Wang

Gracheva

Richmond

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Communication between neurons is largely achieved through chemical synapses, where neurotransmitters are released from synaptic vesicles at presynaptic terminals to activate postsynaptic cells. Exo-and endocytosis are coordinated to replenish the synaptic vesicle pool for sustained neuronal activity. We identified syd-9 (syd, synapse defective), a gene that encodes multiple C2H2 zinc-finger domain-containing proteins specifically required for synaptic function in Caenorhabditis elegans. syd-9 loss-of-function mutants exhibit locomotory defects, a diffuse distribution of synaptic proteins, and decreased synaptic transmission with unaffected neurodevelopment. syd-9 mutants share phenotypic and ultrastructural characteristics with mutants that lack synaptic proteins that are required for endocytosis. syd-9 mutants also display genetic interactions with these endocytotic mutants, suggesting that SYD-9 regulates endocytosis. SYD-9 proteins are enriched in the nuclei of both neuron and muscle cells, but their neuronal expression plays a major role in locomotion. SYD-9 isoforms display a speckle-like expression pattern that is typical of RNAbinding proteins that regulate premRNA splicing. Furthermore, syd-9 functions in parallel with unc-75 (unc, uncoordinated), the C. elegans homologue of the CELF͞BrunoL family protein that regulates mRNA alternative splicing and processing, and is also required specifically for synaptic transmission. We propose that neuronal SYD-9 proteins are previously uncharacterized and specific posttranscriptional regulators of synaptic vesicle endocytosis.BrunoL͞UNC-75 ͉ Caenorhabditis elegans ͉ endocytosis ͉ synaptic function C hemical synapses mediate neuronal communication through the regulated release of neurotransmitters from synaptic vesicles. Extensive studies have focused on the molecular machinery that mediates and regulates exocytosis, the process in which membrane fusion between synaptic vesicles and the plasma membrane leads to neurotransmitter release and endocytosis, the process that recovers synaptic vesicles from the plasma membrane (1, 2).The release of neurotransmitters is stimulated by the influx of Ca 2ϩ at the presynaptic active zones. Protein components of the vesicle membranes (synaptobrevin, SNB) and plasma membranes [syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa)] form a SNARE complex that functions as a minimal fusion machine to drive vesicle fusion (3-5). The formation and conformational change of the SNARE complex requires modulation by other proteins (6-9). Synaptotagmin (SNT) is a vesicle membrane protein that binds to Ca 2ϩ and forms complexes with phospholipids and SNARE complexes. It is a proposed Ca 2ϩ sensor for Ca 2ϩ -dependent exocytosis (10-12). SNT-1 knockout mice display selective loss of Ca 2ϩ -triggered fast exocytosis, and loss of SNT function in Caenorhabditis elegans and Drosophila leads to a large reduction of exocytosis (13,14). Disrupting the function of UNC13͞mUNC13 and UNC-18͞mUNC18 (UNC, uncoordinated) also leads to a reduction...

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Bruno Inhibits the Expression of Mitotic Cyclins during the Prophase I Meiotic Arrest of Drosophila Oocytes

Cited by 90 publications

References 50 publications

Regulation of Cyclin A protein in meiosis and early embryogenesis

Regulation of Cyclin A protein in meiosis and early embryogenesis

Translational regulation of the cell cycle: when, where, how and why?

The C2H2 zinc-finger protein SYD-9 is a putative posttranscriptional regulator for synaptic transmission

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