Ontology highlight
ABSTRACT:
PROVIDER: PRJNA540320 | ENA |
REPOSITORIES: ENA
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Project description:In eukaryotes, up to one-third of cellular proteins are targeted to the endoplasmic reticulum, where they undergo folding, processing, sorting and trafficking to subsequent endomembrane compartments. Targeting to the endoplasmic reticulum has been shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-translationally by the mammalian transmembrane recognition complex of 40 kDa (TRC40) and homologous yeast guided entry of tail-anchored proteins (GET) pathways. Despite the range of proteins that can be catered for by these two pathways, many proteins are still known to be independent of both SRP and GET, so there seems to be a critical need for an additional dedicated pathway for endoplasmic reticulum relay. We set out to uncover additional targeting proteins using unbiased high-content screening approaches. To this end, we performed a systematic visual screen using the yeast Saccharomyces cerevisiae, and uncovered three uncharacterized proteins whose loss affected targeting. We suggest that these proteins work together and demonstrate that they function in parallel with SRP and GET to target a broad range of substrates to the endoplasmic reticulum. The three proteins, which we name Snd1, Snd2 and Snd3 (for SRP-independent targeting), can synthetically compensate for the loss of both the SRP and GET pathways, and act as a backup targeting system. This explains why it has previously been difficult to demonstrate complete loss of targeting for some substrates. Our discovery thus puts in place an essential piece of the endoplasmic reticulum targeting puzzle, highlighting how the targeting apparatus of the eukaryotic cell is robust, interlinked and flexible.
2016-11-30 | GSE85686 | GEO
Project description:Epithelial endoplasmic reticulum stress orchestrates a protective IgA response I
| PRJNA512503 | ENA
Project description:Epithelial endoplasmic reticulum stress orchestrates a protective IgA response II
| PRJNA512502 | ENA
Project description:The unfolded protein response (UPR) is a network of intracellular signaling pathways that supports the ability of the secretory pathway to maintain equilibrium between the load of proteins entering the endoplasmic reticulum (ER) and the protein folding capacity of the ER lumen. Current evidence suggests that human pathogenic fungi rely heavily on this pathway for virulence, but there is limited understanding of the mechanisms involved. The best known functional output of the UPR is transcriptional upregulation of mRNAs involved in ER homeostasis. However, this does not take into account mechanisms of translational regulation that involve differential recruitment of mRNAs to ribosomes. In this study, a global analysis of transcript-specific translational regulation was performed in the pathogenic mold Aspergillus fumigatus to determine the nature and scope of the translational response to ER stress.
2014-01-13 | E-MTAB-2028 | biostudies-arrayexpress
Project description:Endoplasmic reticulum oxidoreductase 1 alpha (ERO1α) is an endoplasmic reticulum stress–related gene, which improves cell perseverance against challenges of high levels of protein misfolding during endoplasmic reticulum stress by retaining good activity of oxidative protein folding. Numerous studies have shown abnormal expression of ERo1α in various diseases, but its downstream target are not fully understood. Our work will help in the elucidation of the downstream molecular mechanism of ERO1α.
2024-04-17 | GSE246899 | GEO
Project description:Localized protein synthesis is a fundamental mechanism for creating distinct subcellular environments. Here we developed a generalizable proximity-specific ribosome profiling strategy that enables global interrogation of translation in defined subcellular locations. We applied this approach to the endoplasmic reticulum (ER) in yeast and mammals. We observed the vast majority of secretory proteins to be co-translationally translocated, including substrates capable of post-translational insertion in vitro. Distinct translocon complexes engaged nascent chains at different points during synthesis. Whereas most proteins engaged the ER immediately following or even before signal sequence (SS) emergence, a class of Sec66-dependent proteins entered with a looped SS conformation. Finally, we observed rapid ribosome exchange into the cytosol following translation termination. These data provide insights into how distinct translocation mechanisms act in concert to promote efficient co-translational recruitment.
2014-11-10 | GSE61012 | GEO
Project description:Endoplasmic reticulum (ER) stress and the unfolded protein response (UPR)
| PRJNA137213 | ENA
Project description:The IRE1a-XBP1 pathway, a conserved adaptive response to the unfolded protein response, is indispensable for development of the secretory cells. It maintains endoplasmic reticulum homeostasis by enhancing protein folding and the secretory capacity of the cells. Here, we used a modified ChIP-seq protocol (ChIPmentation) to investigate the genome-wide binding events of the transcription factor XBP1 in differentiated mouse Th2 cells.
2018-10-06 | E-MTAB-6327 | biostudies-arrayexpress
Project description:The goals of this study are to compare transcriptome profiling (mRNA level) and signaling pathways between the control and ablating LSD1, the control and ablating G9a, the control and co-ablating LSD1 and G9a. We found pathways in apoptosis, endoplasmic reticulum stress and unfolded protein response were obviously changed in these groups, which are important for esophageal cancer therapy.
2022-05-01 | GSE173666 | GEO
Project description:The SND proteins constitute an alternative targeting route to the endoplasmic reticulum
| PRJNA339062 | ENA