ArticleNucleic acids research2014
The Drosophila RNA-binding protein HOW controls the stability of dgrasp mRNA in the follicular epithelium.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Held out wings RNA binding activity in the cytoplasm during early spermatogenesis.Communications biology · 2026Article
- Investigating the cellular functions of β-Glucosidases for synthesis of lignocellulose-degrading enzymes inEngineering microbiology · 2023Article
- The Arp2/3 complex and the formin, Diaphanous, are both required to regulate the size of germline ring canals in the developing egg chamber.Developmental biology · 2020Article
- The Misshapen kinase regulates the size and stability of the germline ring canals in the Drosophila egg chamber.Developmental biology · 2018Article
- Molecular basis for asymmetry sensing of siRNAs by the Drosophila Loqs-PD/Dcr-2 complex in RNA interference.Nucleic acids research · 2017Article
- Homology directed repair is unaffected by the absence of siRNAs in Drosophila melanogaster.Nucleic acids research · 2016Article
- GRASP: A Multitasking Tether.Frontiers in cell and developmental biology · 2016Review
- Loss of a Clueless-dGRASP complex results in ER stress and blocks Integrin exit from the perinuclear endoplasmic reticulum in Drosophila larval muscle.Biology open · 2015Article
- A stress assembly that confers cell viability by preserving ERES components during amino-acid starvation.eLife · 2014Article
- Leigh syndrome in Drosophila melanogaster: morphological and biochemical characterization of Surf1 post-transcriptional silencing.The Journal of biological chemistry · 2014Article
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4 authors at 1 institution in 1 country.
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Abstract
Post-transcriptional regulation of RNA stability and localization underlies a wide array of developmental processes, such as axon guidance and epithelial morphogenesis. In Drosophila, ectopic expression of the classically Golgi peripheral protein dGRASP at the plasma membrane is achieved through its mRNA targeting at key developmental time-points, in a process critical to follicular epithelium integrity. However, the trans-acting factors that tightly regulate the spatio-temporal dynamics of dgrasp are unknown. Using an in silico approach, we identified two putative HOW Response Elements (HRE1 and HRE2) within the dgrasp open reading frame for binding to Held Out Wings (HOW), a member of the Signal Transduction and Activation of RNA family of RNA-binding proteins. Using RNA immunoprecipitations, we confirmed this by showing that the short cytoplasmic isoform of HOW binds directly to dgrasp HRE1. Furthermore, HOW loss of function in vivo leads to a significant decrease in dgrasp mRNA levels. We demonstrate that HRE1 protects dgrasp mRNA from cytoplasmic degradation, but does not mediate its targeting. We propose that this binding event promotes the formation of ribonucleoprotein particles that ensure dgrasp stability during transport to the basal plasma membrane, thus enabling the local translation of dgrasp for its roles at non-Golgi locations.
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