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The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins

ABSTRACT: The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins

PROVIDER: PRJNA449388 | ENA |

REPOSITORIES: ENA

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The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins

Project description:The endoplasmic reticulum (ER) supports biosynthesis of proteins with diverse transmembrane domain (TMD) lengths and hydrophobicity. Features in transmembrane domains such as charged residues in ion channels are often functionally important, but could pose a challenge during cotranslational membrane insertion and folding. Our systematic proteomic approaches in both yeast and human cells revealed that the ER membrane protein complex (EMC) binds to and promotes the biogenesis of a range of multipass transmembrane proteins, with a particular enrichment for transporters. Proximity-specific ribosome profiling demonstrates that the EMC engages clients cotranslationally and immediately following clusters of TMDs enriched for charged residues. The EMC can remain associated after completion of translation, which both protects clients from premature proteasomal degradation and allows recruitment of substrate-specific and general chaperones. Thus, the EMC broadly enables the biogenesis of multipass transmembrane proteins containing destabilizing features, thereby mitigating the trade-off between function and stability.

2018-05-29 | GSE112891 | GEO

The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins.

Project description:The endoplasmic reticulum (ER) supports biosynthesis of proteins with diverse transmembrane domain (TMD) lengths and hydrophobicity. Features in transmembrane domains such as charged residues in ion channels are often functionally important, but could pose a challenge during cotranslational membrane insertion and folding. Our systematic proteomic approaches in both yeast and human cells revealed that the ER membrane protein complex (EMC) binds to and promotes the biogenesis of a range of multipass transmembrane proteins, with a particular enrichment for transporters. Proximity-specific ribosome profiling demonstrates that the EMC engages clients cotranslationally and immediately following clusters of TMDs enriched for charged residues. The EMC can remain associated after completion of translation, which both protects clients from premature degradation and allows recruitment of substrate-specific and general chaperones. Thus, the EMC broadly enables the biogenesis of multipass transmembrane proteins containing destabilizing features, thereby mitigating the trade-off between function and stability.

| S-EPMC5995541 | biostudies-literature

VAP-A and its binding partner CERT drive biogenesis of RNA-containing extracellular vesicles at ER membrane contact sites

Project description:RNA transfer via extracellular vesicles (EVs) influences cell phenotypes; however, lack of information regarding biogenesis of RNA-containing EVs has limited progress in the field. Here, we identify endoplasmic reticulum membrane contact sites (ER MCS) as platforms for generation of RNA-containing EVs. We identify a subpopulation of small EVs that is highly enriched in RNA and regulated by the ER MCS linker protein VAP-A. Functionally, VAP-A-regulated EVs are critical for miR-100 transfer between cells and in vivo tumor formation. Lipid analysis of VAP-A-knockdown EVs revealed reductions in the EV biogenesis lipid ceramide. Knockdown of the VAP-A-binding ceramide transfer protein CERT led to similar defects in EV RNA content. Imaging experiments revealed that VAP-A promotes lumenal filling of multivesicular bodies (MVBs). CERT localizes to MVBs, and the ceramide-generating enzyme neutral sphingomyelinase 2 colocalizes with VAP-A-positive ER. We propose that ceramide transfer via VAP-A-CERT linkages drives biogenesis of a select RNA-containing population.

2022-04-05 | GSE188223 | GEO

RNA messengers translated at the ER membrane

Project description:In order to identify what RNA messengers are being translated at the ER membrane, membrane-associated polysomes were separated from free polysomes by subcellular fractionation of WT and delta-egd1/delta-egd2 yeast strains and associated RNA was isolated and then identified by microarray analysis. Set of arrays that are part of repeated experiments

2013-04-05 | E-GEOD-45795 | biostudies-arrayexpress

RNA messengers translated at the ER membrane

2013-04-05 | GSE45795 | GEO

Environmental influences on Streptococcus sanguinis membrane vesicle biogenesis

Project description:Environmental influences on Streptococcus sanguinis membrane vesicle biogenesis

| PRJNA937727 | ENA

Environmental influences on Streptococcus sanguinis membrane vesicle biogenesis

Project description:To look for transcriptomic changes that resulted in membrane vesicle biogenesis, we performed RNA sequencing on S.sanguinis in different culture and community conditions We then examined three separate differential expression analyses, as well as correlated the phenotypic vesicle quantification with normalized count data across all samples.

2023-03-31 | GSE225861 | GEO

VAP-A and its binding partner CERT drive biogenesis of RNA-containing extracellular vesicles at ER membrane contact sites

Project description:VAP-A and its binding partner CERT drive biogenesis of RNA-containing extracellular vesicles at ER membrane contact sites

| PRJNA777941 | ENA

The proteasome biogenesis regulator Rpn4 cooperates with the unfolded protein response to promote ER stress resistance

Project description:Misfolded proteins in the endoplasmic reticulum (ER) activate the unfolded protein response (UPR), which enhances protein folding to restore homeostasis. Additional pathways respond to ER stress, but how they help counteract protein misfolding is incompletely understood. Here, we develop a titratable system for the induction of ER stress in yeast to enable a genetic screen for factors that augment stress resistance independently of the UPR. We identify the proteasome biogenesis regulator Rpn4 and show that it cooperates with the UPR. Rpn4 abundance increases during ER stress, first by a post-transcriptional, then by a transcriptional mechanism. Induction of RPN4 transcription is triggered by cytosolic mislocalization of secretory proteins, is mediated by multiple signaling pathways and accelerates clearance of misfolded proteins from the cytosol. Thus, Rpn4 and the UPR are complementary elements of a modular cross-compartment response to ER stress.

2019-03-13 | PXD012867 | Pride

The Endoplasmic Reticulum (ER) Kinase PERK Interacts with the Oxidoreductase ERO1 to Mediate Metabolic Adaptation to ER Stress

Project description:Our study has shown that during the initiation of ER-stress the oxidoreductase ERO1⍺ covalently interacts with PERK at the MERCs domain. The complex promotes oxidization of MERC proteins and controls mitochondrial dynamics to adapt to new energy needs.

2022-12-06 | PXD038562 | JPOST Repository

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