scholarly journals HELZ directly interacts with CCR4–NOT and causes decay of bound mRNAs

2019 ◽  
Vol 2 (5) ◽  
pp. e201900405 ◽  
Author(s):  
Aoife Hanet ◽  
Felix Räsch ◽  
Ramona Weber ◽  
Vincenzo Ruscica ◽  
Maria Fauser ◽  
...  
Keyword(s):  
Nervous System ◽  
Drosophila Melanogaster ◽  
Mrna Decay ◽  
Low Complexity ◽  
Tata Box ◽  
Translational Repression ◽  
Terminal Part ◽  
Expression Of Genes ◽  
Catabolite Repressor

Eukaryotic superfamily (SF) 1 helicases have been implicated in various aspects of RNA metabolism, including transcription, processing, translation, and degradation. Nevertheless, until now, most human SF1 helicases remain poorly understood. Here, we have functionally and biochemically characterized the role of a putative SF1 helicase termed “helicase with zinc-finger,” or HELZ. We discovered that HELZ associates with various mRNA decay factors, including components of the carbon catabolite repressor 4-negative on TATA box (CCR4–NOT) deadenylase complex in human and Drosophila melanogaster cells. The interaction between HELZ and the CCR4–NOT complex is direct and mediated by extended low-complexity regions in the C-terminal part of the protein. We further reveal that HELZ requires the deadenylase complex to mediate translational repression and decapping-dependent mRNA decay. Finally, transcriptome-wide analysis of Helz-null cells suggests that HELZ has a role in the regulation of the expression of genes associated with the development of the nervous system.

scholarly journals A UPF1 variant drives conditional remodeling of nonsense-mediated mRNA decay

2021 ◽  
Author(s):  
Sarah E. Fritz ◽  
Soumya Ranganathan ◽  
J. Robert Hogg
Keyword(s):  
Gene Expression ◽  
Mrna Decay ◽  
Gene Expression Regulation ◽  
Translation Termination ◽  
Translational Repression ◽  
The Core ◽  
Human Genes ◽  
Rna Quality Control ◽  
Nonsense Mediated Mrna Decay

AbstractThe nonsense-mediated mRNA decay (NMD) pathway monitors translation termination to degrade transcripts with premature stop codons and regulate thousands of human genes. Due to the major role of NMD in RNA quality control and gene expression regulation, it is important to understand how the pathway responds to changing cellular conditions. Here we show that an alternative mammalian-specific isoform of the core NMD factor UPF1, termed UPF1LL, enables condition-dependent remodeling of NMD specificity. UPF1LL associates more stably with potential NMD target mRNAs than the major UPF1SL isoform, expanding the scope of NMD to include many transcripts normally immune to the pathway. Unexpectedly, the enhanced persistence of UPF1LL on mRNAs supports induction of NMD in response to rare translation termination events. Thus, while canonical NMD is abolished by translational repression, UPF1LL activity is enhanced, providing a mechanism to rapidly rewire NMD specificity in response to cellular stress.

scholarly journals Drosophila Zic family member odd-paired is needed for adult post-ecdysis maturation

Open Biology ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 190245
Author(s):  
Eléanor Simon ◽  
Sergio Fernández de la Puebla ◽  
Isabel Guerrero
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Transcription Factor ◽  
Drosophila Melanogaster ◽  
Family Member ◽  
Ectopic Expression ◽  
Functional Conservation ◽  
The Central Nervous System ◽  
Behavioural Sequence

Specific neuropeptides regulate in arthropods the shedding of the old cuticle (ecdysis) followed by maturation of the new cuticle. In Drosophila melanogaster , the last ecdysis occurs at eclosion from the pupal case, with a post-eclosion behavioural sequence that leads to wing extension, cuticle stretching and tanning. These events are highly stereotyped and are controlled by a subset of crustacean cardioactive peptide (CCAP) neurons through the expression of the neuropeptide Bursicon (Burs). We have studied the role of the transcription factor Odd-paired (Opa) during the post-eclosion period. We report that opa is expressed in the CCAP neurons of the central nervous system during various steps of the ecdysis process and in peripheral CCAP neurons innerving the larval muscles involved in adult ecdysis. We show that its downregulation alters Burs expression in the CCAP neurons. Ectopic expression of Opa, or the vertebrate homologue Zic2 , in the CCAP neurons also affects Burs expression, indicating an evolutionary functional conservation. Finally, our results show that, independently of its role in Burs regulation, Opa prevents death of CCAP neurons during larval development.

scholarly journals Role of the DSC1 Channel in Regulating Neuronal Excitability in Drosophila melanogaster: Extending Nervous System Stability under Stress

PLoS Genetics ◽  
2013 ◽  
Vol 9 (3) ◽  
pp. e1003327 ◽  
Author(s):  
Tianxiang Zhang ◽  
Zhe Wang ◽  
Lingxin Wang ◽  
Ningguang Luo ◽  
Lan Jiang ◽  
...  
Keyword(s):  
Nervous System ◽  
Drosophila Melanogaster ◽  
Neuronal Excitability ◽  
System Stability

scholarly journals The role of the BR-C locus on the expression of genes located at the ecdysone-regulated 3C puff of Drosophila melanogaster

1995 ◽  
Vol 49 (3) ◽  
pp. 161-171 ◽  
Author(s):  
Pier Paolo D'Avino ◽  
Stefania Crispi ◽  
Lino C. Polito ◽  
Maria Furia
Keyword(s):  
Drosophila Melanogaster ◽  
Expression Of Genes

scholarly journals The C-Terminal RGG Domain of Human Lsm4 Promotes Processing Body Formation Stimulated by Arginine Dimethylation

2016 ◽  
Vol 36 (17) ◽  
pp. 2226-2235 ◽  
Author(s):  
Marcos Arribas-Layton ◽  
Jaclyn Dennis ◽  
Eric J. Bennett ◽  
Christian K. Damgaard ◽  
Jens Lykke-Andersen
Keyword(s):  
Posttranslational Modifications ◽  
Mrna Decay ◽  
Low Complexity ◽  
Translational Repression ◽  
Processing Bodies ◽  
Content Type ◽  
Rich Domain ◽  
Pb Accumulation ◽  
Processing Body ◽  
Protein Components

Processing bodies (PBs) are conserved cytoplasmic aggregations of translationally repressed mRNAs assembled with mRNA decay factors. The aggregation of mRNA-protein (mRNP) complexes into PBs involves interactions between low-complexity regions of protein components of the mRNPs. InSaccharomyces cerevisiae, the carboxy (C)-terminal Q/N-rich domain of the Lsm4 subunit of the Lsm1-7 complex plays an important role in PB formation, but the C-terminal domain of Lsm4 in most eukaryotes is an RGG domain rather than Q/N rich. Here we show that the Lsm4 RGG domain promotes PB accumulation in human cells and that symmetric dimethylation of arginines within the RGG domain stimulates this process. A mutant Lsm4 protein lacking the RGG domain failed to rescue PB formation in cells depleted of endogenous Lsm4, although this mutant protein retained the ability to assemble with Lsm1-7, associate with decapping factors, and promote mRNA decay and translational repression. Mutation of the symmetrically dimethylated arginines within the RGG domain impaired the ability of Lsm4 to promote PB accumulation. Depletion of PRMT5, the primary protein arginine methyltransferase responsible for symmetric arginine dimethylation, including Lsm4, resulted in loss of PBs. We also uncovered the histone acetyltransferase 1 (HAT1)-RBBP7 lysine acetylase complex as an interaction partner of the Lsm4 RGG domain but found no evidence of a role for this complex in PB metabolism. Together, our findings suggest a stimulatory role for posttranslational modifications in PB accumulation and raise the possibility that mRNP dynamics are posttranslationally regulated.

scholarly journals Squeezing out in a “tug of war”: The role of myosin in neural stem cell delamination

2017 ◽  
Vol 216 (5) ◽  
pp. 1215-1218
Author(s):  
Clara Sidor ◽  
Katja Röper
Keyword(s):  
Stem Cells ◽  
Nervous System ◽  
Drosophila Melanogaster ◽  
Stem Cell ◽  
Spatial Resolution ◽  
Molecular Mechanisms ◽  
Single Cells ◽  
Apical Constriction ◽  
Temporal And Spatial

Neural stem cells or neuroblasts in the Drosophila melanogaster embryo delaminate as single cells from the embryonic epidermis to give rise to the nervous system. Using this accessible system to examine the molecular mechanisms of cell ingression at a high temporal and spatial resolution, in this issue, Simões et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201608038) reveal that myosin-driven anisotropic junction loss and apical constriction are the main drivers of this process.

scholarly journals RGG-motif protein Sbp1 is required for Processing body (P-body) disassembly

2021 ◽  
Author(s):  
Raju Roy ◽  
Ishwarya Achappa Kuttanda ◽  
Nupur Bhatter ◽  
Purusharth I Rajyaguru
Keyword(s):  
Mrna Decay ◽  
Glucose Deprivation ◽  
Low Complexity ◽  
Wild Type ◽  
Processing Bodies ◽  
P Bodies ◽  
Rna Granules ◽  
Processing Body ◽  
Mrna Fate

AbstractRNA granules are conserved mRNP complexes that play an important role in determining mRNA fate by affecting translation repression and mRNA decay. Processing bodies (P-bodies) harbor enzymes responsible for mRNA decay and proteins involved in modulating translation. Although many proteins have been identified to play a role in P-body assembly, a bonafide disassembly factor remains unknown. In this report, we identify RGG-motif translation repressor protein Sbp1 as a disassembly factor of P-bodies. Disassembly of Edc3 granules but not the Pab1 granules (a conserved stress granule marker) that arise upon sodium azide and glucose deprivation stress are defective in Δsbp1. Disassembly of other P-body proteins such as Dhh1 and Scd6 is also defective in Δsbp1. Complementation experiments suggest that the wild type Sbp1 but not an RGG-motif deletion mutant rescues the Edc3 granule disassembly defect in Δsbp1. We observe that purified Edc3 forms assemblies, which is promoted by the presence of RNA and NADH. Strikingly, addition of purified Sbp1 leads to significantly decreased Edc3 assemblies. Although low complexity sequences have been in general implicated in assembly, our results reveal the role of RGG-motif (a low-complexity sequence) in the disassembly of P-bodies.

Proneural genes influence gliogenesis in Drosophila

Development ◽  
1995 ◽  
Vol 121 (2) ◽  
pp. 429-438 ◽  
Author(s):  
A. Giangrande
Keyword(s):  
Nervous System ◽  
Drosophila Melanogaster ◽  
Genetic Analysis ◽  
Glial Cells ◽  
Sensory Organ ◽  
Loss Of Function ◽  
Sensory Organs ◽  
Genetic Pathway ◽  
Organ Differentiation

Fly glial cells in the wing peripheral nervous system of Drosophila melanogaster originate from underlying epithelial cells. Two findings indicate that gliogenesis is closely associated with neurogenesis. First, it only occurs in regions that also give rise to sensory organs. Second, in mutants that induce the development of ectopic sensory organs glial cells develop at new positions. These findings prompted a genetic analysis to establish whether glial and sensory organ differentiation depend on the same genes. Loss of function mutations of the achaete-scute complex lead to a significant reduction of sensory bristles and glial cells. Genes within the complex affect gliogenesis with different strength and display some functional redundancy. Thus, neurogenesis and gliogenesis share the same genetic pathway. Despite these similarities, however, the mechanism of action of the achaete-scute complex seems to be different in the two processes. Neural precursors express products of the complex, therefore the role of these genes on neurogenesis is direct. However, markers specific to glial cells do not colocalize with products of the achaete-scute complex, showing that the complex affects gliogenesis indirectly. These observations lead to the hypothesis that gliogenesis is induced by the presence of sensory organ cells, either the precursor or its progeny.

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