Drosophila vigilin, DDP1, localises to the cytoplasm and associates to the rough endoplasmic reticulum

Batlle, Marta; Marsellach, Xavi; Huertas, Dori; Azorı́n, Fernando

doi:10.1016/j.bbagrm.2010.10.005

Cited by 13 publications

(22 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Cytoplasmic vigilin plays a key role in mRNA stabilization and positively regulates translation, notably in response to stress (17)(18)(19)46). Interestingly, we observed that CF airway neutrophils undergo marked changes in their transcriptional profile compared with CF blood neutrophils (Laval et al, manuscript in preparation), consistent with reprogramming (3,39).…”

Section: Discussionsupporting

confidence: 63%

“…Vigilin is an RNA-binding protein with nuclear and cytoplasmic localizations, the latter being linked to anabolic activity in the form of increased RNA translation (17)(18)(19). Recent evidence from our group (J. Laval, M. Makam, D. Diaz, M. Preininger, M. Miglianico, L.A. Herzenberg, and R. Tirouvanziam, manuscript in preparation) and other investigators (39) suggests that CF airway neutrophils are transcriptionally and translationally active.…”

Section: Recruitment Of Neutrophils To Cf Airways Is Associated With mentioning

confidence: 99%

“…Using imaging flow cytometry (ImageStreamX platform; Amnis), we also characterized the expression and cytoplasmic localization of the conserved RNA-binding protein vigilin in blood and airway neutrophils. Vigilin has been associated with anabolic activity as a positive regulator of mRNA translation in multiple eukaryotic organisms, including humans (17)(18)(19). Simultaneously to vigilin, we characterized the expression of the LC3 protein, previously linked to multiple catabolic activities, including autophagy, phagocytosis, and the exocytosis of proteolytic enzymes (20)(21)(22)(23).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Metabolic Adaptation of Neutrophils in Cystic Fibrosis Airways Involves Distinct Shifts in Nutrient Transporter Expression

Laval

Touhami

Herzenberg

et al. 2013

The Journal of Immunology

View full text Add to dashboard Cite

Inflammatory conditions can profoundly alter human neutrophils, a leukocyte subset generally viewed as terminally differentiated and catabolic. In cystic fibrosis (CF) patients, neutrophils recruited to CF airways show active exocytosis and sustained phosphorylation of prosurvival, metabolic pathways. Because the CF airway lumen is also characterized by high levels of free glucose and amino acids, we compared surface expression of Glut1 (glucose) and ASCT2 (neutral amino acids) transporters, as well as that of PiT1 and PiT2 (inorganic phosphate transporters), in blood and airway neutrophils, using specific retroviral envelope-derived ligands. Neither nutrient transporter expression nor glucose uptake was altered on blood neutrophils from CF patients compared with healthy controls. Notably, however, airway neutrophils of CF patients had higher levels of PiT1 and Glut1 and increased glucose uptake compared with their blood counterparts. Based on primary granule exocytosis and scatter profiles, CF airway neutrophils could be divided into two subsets, with one of the subsets characterized by more salient increases in Glut1, ASCT2, PiT1, and PiT2 expression. Moreover, in vitro exocytosis assays of blood neutrophils suggest that surface nutrient transporter expression is not directly associated with primary (or secondary) granule exocytosis. Although expression of nutrient transporters on CF blood or airway neutrophils was not altered by genotype, age, gender, or Pseudomonas aeruginosa infection, oral steroid treatment decreased Glut1 and PiT2 levels in blood neutrophils. Thus, neutrophils recruited from blood into the CF airway lumen display augmented cell surface nutrient transporter expression and glucose uptake, consistent with metabolic adaptation.

show abstract

Section: Discussionsupporting

confidence: 63%

Section: Recruitment Of Neutrophils To Cf Airways Is Associated With mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Metabolic Adaptation of Neutrophils in Cystic Fibrosis Airways Involves Distinct Shifts in Nutrient Transporter Expression

Laval

Touhami

Herzenberg

et al. 2013

The Journal of Immunology

View full text Add to dashboard Cite

show abstract

“…Polyclonal rat aWOC (IF: 1/500) and rabbit aROW (WB: 1/10,000, ChIP/IP: 1 ml) antibodies were raised against recombinant proteins aa230-626 and aa588-956, respectively. Other antibodies used are described in the indicated references: rat aHP1c (WB: 1/10,000, IF: 1/500, ChIP/IP: 1 ml), aHP1b (WB: 1/ 10,000, ChIP/IP: 1 ml) and aROW (WB: 1/10,000, IF: 1/400, ChIP/IP: 1 ml) 18 , rabbit aWOC (WB: 1/10,000, ChIP/IP: 1 ml) 62 , rabbit and rat aDDP1 (ChIP/IP: 1 ml) 63 , rabbit adDsk2 (WB: 1/12,000, IF: 1/1,000, ChIP/IP: 1 ml) 16 , mouse ap54 (WB: 1/50) 64 , rabbit aNELF-E (WB: 1/500, ChIP/IP: 3 ml) 65 and rabbit aRPB3 (WB: 1/1,500, ChIP: 15 ml) 26 . Commercially available antibodies used were as follows: rabbit aH3K4me3 (Abcam, ab8580, ChIP: 1 ml), rabbit aIIoser5 (Abcam, ab5131, ChIP: 3 ml), rabbit aBre1 (NOVUS, 40280002, WB: 1/1,000, ChIP: 2 ml) and aRad6 (SANTA CRUZ, sc-30078, WB: 1/500, ChIP: 2 ml), mouse aGST (glutathione S-transferase; Novagen, 71097-3, WB: 1/10,000), mouse aGFP (Roche, 1814460, IF: 1/50), mouse aH2Bub1 (Millipore, 05-1312, WB: 1/4,000, ChIP/IP: 1 ml), mouse aTubulin (Millipore, MAB3408, WB: 1/2,000), rabbit aActin (Sigma, A2066, WB: 1/10,000), mouse aV5 (Invitrogen, 460705, WB: 1/5,000), mouse aUbiquitin (SANTA CRUZ, sc-8017, WB: 1/500), rabbit aPanAc (Abcam, Ab193-100, ChIP: 1 ml) and rabbit aH4Ac (Millipore, no.…”

Section: Methodsmentioning

confidence: 99%

dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

et al. 2015

Self Cite

View full text Add to dashboard Cite

dDsk2 is a conserved extraproteasomal ubiquitin receptor that targets ubiquitylated proteins for degradation. Here we report that dDsk2 plays a nonproteolytic function in transcription regulation. dDsk2 interacts with the dHP1c complex, localizes at promoters of developmental genes and is required for transcription. Through the ubiquitin-binding domain, dDsk2 interacts with H2Bub1, a modification that occurs at dHP1c complex-binding sites. H2Bub1 is not required for binding of the complex; however, dDsk2 depletion strongly reduces H2Bub1. Co-depletion of the H2Bub1 deubiquitylase dUbp8/Nonstop suppresses this reduction and rescues expression of target genes. RNA polymerase II is strongly paused at promoters of dHP1c complex target genes and dDsk2 depletion disrupts pausing. Altogether, these results suggest that dDsk2 prevents dUbp8/Nonstop-dependent H2Bub1 deubiquitylation at promoters of dHP1c complex target genes and regulates RNA polymerase II pausing. These results expand the catalogue of nonproteolytic functions of ubiquitin receptors to the epigenetic regulation of chromatin modifications.

show abstract

“…Depending on their subcellular distribution, mRNAs may be exposed to distinct pools of regulatory factors and translational components, which may affect protein production. Various translational regulators 48–51 , ribonucleases 52–54 and RNA-binding proteins 43,55 localize to the ER to promote specialized functions. For example, an emerging body of work demonstrates that small interfering RNA (siRNA)- and microRNA (miRNA)-mediated silencing is highly dependent on the ER; for both transfected siRNAs and endogenous miRNAs, the critical processes of RNA-induced silencing complex (RISC) loading, mRNA binding and Argonaute 2-mediated processing occur in association with the ER membrane 51,56 .…”

Section: Compartment-selective Mrna Translationmentioning

confidence: 99%

Diversity and selectivity in mRNA translation on the endoplasmic reticulum

Reid

Nicchitta

2015

Nat Rev Mol Cell Biol

206

173

View full text Add to dashboard Cite

Pioneering electron microscopy studies defined two primary populations of ribosomes in eukaryotic cells: one freely dispersed through the cytoplasm and the other bound to the surface of the endoplasmic reticulum (ER). Subsequent investigations revealed a specialized function for each population, with secretory and integral membrane protein-encoding mRNAs translated on ER-bound ribosomes, and cytosolic protein synthesis was widely attributed to free ribosomes. Recent findings have challenged this view, and transcriptome-scale studies of mRNA distribution and translation have now demonstrated that ER-bound ribosomes also function in the translation of a large fraction of mRNAs that encode cytosolic proteins. These studies suggest a far more expansive role for the ER in transcriptome expression, where membrane and secretory protein synthesis represents one element of a multifaceted and dynamic contribution to post-transcriptional gene expression.

show abstract

Drosophila vigilin, DDP1, localises to the cytoplasm and associates to the rough endoplasmic reticulum

Cited by 13 publications

References 45 publications

Metabolic Adaptation of Neutrophils in Cystic Fibrosis Airways Involves Distinct Shifts in Nutrient Transporter Expression

Metabolic Adaptation of Neutrophils in Cystic Fibrosis Airways Involves Distinct Shifts in Nutrient Transporter Expression

dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

Diversity and selectivity in mRNA translation on the endoplasmic reticulum

Contact Info

Product

Resources

About