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Systemwide effects of ER-intracellular membrane contact site disturbance in primary endothelial cells

ABSTRACT: Systemwide effects of ER-intracellular membrane contact site disturbance in primary endothelial cells

PROVIDER: PRJNA945344 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR23875964_1.fastq.gz	Fastqsanger.gz
	SRR23875964_2.fastq.gz	Fastqsanger.gz
	SRR23875965_1.fastq.gz	Fastqsanger.gz
	SRR23875965_2.fastq.gz	Fastqsanger.gz
	SRR23875966_1.fastq.gz	Fastqsanger.gz

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Systemwide effects of ER-intracellular membrane contact site disturbance in primary endothelial cells

Project description:We investigate how the double knock down of VAPA and VAPB affected the macromolecule profile of human umbilical vein endothelial cells by transcriptomic and lipidomic profiling

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BRD4-mediated ER membrane contact creates functionally distinct mitochondrial subtypes

Project description:BRD4-mediated ER membrane contact creates functionally distinct mitochondrial subtypes

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BRD4-mediated ER membrane contact creates functionally distinct mitochondrial subtypes

Project description:BRD4-mediated ER membrane contact creates functionally distinct mitochondrial subtypes

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BRD4-mediated ER membrane contact creates functionally distinct mitochondrial subtypes

Project description:Inter-organellar communication is critical for cellular metabolism. One of the most abundant inter-organellar interactions occurs at the endoplasmic reticulum and mitochondria contact sites (ERMCSs). However, an understanding of the mechanisms governing ERMCS regulation and their roles in cellular metabolism is limited by a lack of tools that permit temporal induction and reversal. Through screening approaches, we identified fedratinib, an FDA-approved drug that dramatically increases ERMCS abundance by inhibiting the epigenetic modifier BRD4. Fedratinib rapidly and reversibly modulates mitochondrial and ER morphology, induces a distinct ER-mitochondria envelopment structure, and alters metabolic homeostasis. Moreover, ERMCS modulation depends on mitochondrial electron transport chain complex III function. Comparison of fedratinib activity to other reported inducers of ERMCSs revealed common mechanisms of induction and function, providing clarity to a growing body of experimental observations. In total, our results uncovered a novel epigenetic signaling pathway and an endogenous metabolic regulator that connects ERMCSs and cellular metabolism.

2026-03-25 | GSE280900 | GEO

PDZD8 interacts with Protrudin and Rab7 to form an ER-late endosome membrane contact site that recruits mitochondria

Project description:Endosomes regulate a plethora of cellular processes including signaling, nutrient status and organelle quality control by controlling the fate of material entering the cells. Endosomes undergo a process of maturation which specifies whether material will be shuttled back to the cell surface or degraded by the lysosome. Nevertheless, a complete inventory of factors regulating endosomal maturation is still lacking. Recently, membrane contact sites (MCSs) between the endoplasmic reticulum (ER) and endosomes have emerged as important players in endosomal sorting, dynamics and motility. Here, we identify the ER transmembrane protein PDZD8 as a new Rab7 effector that, together with the MCS component Protrudin, forms an ER-late endosome MCS. At these ER-late endosome MCSs, PDZD8 also recruits mitochondria to form a three-way contact. Our data suggest that the PDZD8/Protrudin-Rab7 MCS functions to facilitate an early stage of late endosome maturation.

2020-06-02 | PXD015523 | Pride

BRD4-mediated ER membrane contact creates functionally distinct mitochondrial subtypes

Project description:Inter-organellar communication is critical for cellular metabolic homeostasis. One of the most abundant inter-organellar interactions are those at the endoplasmic reticulum and mitochondria contact sites (ERMCS). However, a detailed understanding of the mechanisms governing ERMCS regulation and their roles in cellular metabolism are limited by a lack of tools that permit temporal induction and reversal. Through unbiased screening approaches, we identified fedratinib, an FDA-approved drug, that dramatically increases ERMCS abundance by inhibiting the epigenetic modifier BRD4. Fedratinib rapidly and reversibly modulates mitochondrial and ER morphology and alters metabolic homeostasis. Moreover, ERMCS modulation depends on mitochondria electron transport chain complex III function. Comparison of fedratinib activity to other reported inducers of ERMCS revealed common mechanisms of induction and function, providing clarity and union to a growing body of experimental observations. In total, our results uncovered a novel epigenetic signaling pathway and an endogenous metabolic regulator that connects ERMCS and cellular metabolism.

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Human VAPome Analysis Reveals MOSPD1 and MOSPD3 as Membrane Contact Site Proteins Interacting with FFAT-Related FFNT Motifs

Project description:Membrane contact sites (MCS) are intracellular regions where two organelles come closer to exchange information and material. The majority of the endoplasmic reticulum (ER) MCS are attributed to the ER-localized tether proteins VAPA, VAPB, and MOSPD2. These recruit other proteins to the ER by interacting with their FFAT motifs. Here, we describe MOSPD1 and MOSPD3 as ER-localized tethers interacting with FFAT motif-containing proteins. Using BioID, we identify proteins interacting with VAP and MOSPD proteins and find that MOSPD1 and MOSPD3 prefer unconventional FFAT-related FFNT (two phenylalanines [FF] in a neutral tract) motifs. Moreover, VAPA/VAPB/MOSPD2 and MOSPD1/MOSPD3 assemble into two separate ER-resident complexes to interact with FFAT and FFNT motifs, respectively. Because of their ability to interact with FFNT motifs, MOSPD1 and MOSPD3 could form MCS between the ER and other organelles. Collectively, these findings expand the VAP family of proteins and highlight two separate complexes in control of interactions between intracellular compartments.

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APEX2 proximity labeling of PI(3)P dependent ER and early endosome membrane contact tether proteins

Project description:To understand the nature of ER and early endosome membrane contact site, we capitalized the MTM1 knock out (KO) HeLa cells that do not dissociate the ER and early endosome membrane contact upon nutrient starvation. By using the Doxycyclin inducible APEX2 fused Rab5A (early endosome marker) expressing stable cell lines of wildtype (WT) or KO cells, early endsome proximity proteins were acutely biotinyated during starvation. Subsequent biochemical fractionation were conducted to enrich ER membrane and biotinylated proteins were furhter enriched for Mass spectrometry analysis.

2023-01-06 | PXD033846 | Pride

The Legionella-driven PtdIns(4)P gradient at LCV-ER membrane contact sites promotes Vap-, OSBP and Sac1-dependent pathogen vacuole remodeling

Project description:The causative agent of Legionnaires’ disease, Legionella pneumophila, governs interactions with host cells by secreting ca. 330 different “effector” proteins. The facultative intracellular bacteria replicate in macrophages and amoeba within a unique compartment, the Legionella-containing vacuole (LCV). Hallmarks of LCV formation are the phosphoinositide (PI) lipid conversion from PtdIns(3)P to PtdIns(4)P, fusion with endoplasmic reticulum (ER)-derived vesicles and a tight association with the ER. Proteomics of purified LCVs revealed the presence of membrane contact sites (MCS) proteins implicated in lipid exchange. Using dually fluorescence-labeled Dictyostelium discoideum amoeba, we reveal that the VAMP-associated protein (Vap), the PtdIns(4)P 4-phosphatase Sac1, and the large fusion GTPase Sey1/atlastin-3 localize to the ER, but not to the LCV membrane, and these ER-resident proteins promote intracellular replication of L. pneumophila and LCV remodeling. Moreover, oxysterol binding proteins (OSBPs) exclusively localize to the ER (OsbH) or the LCV membrane (OsbK), respectively, and promote (OsbH) or restrict (OsbK) intracellular replication of L. pneumophila and LCV expansion. Furthermore, the PtdIns(4)P-subverting L. pneumophila effectors LepB and SidC also promote LCV remodeling. Taken together, the Legionella-driven PtdIns(4)P gradient at LCV-ER MCSs promotes Vap-, OSBP- and Sac1-dependent pathogen vacuole remodeling.

2023-02-21 | PXD034490 | Pride

TraB is a component of the ER-Mitochondrial contact site regulating ER-Mitochondrial interaction and mitophagy

Project description:ER-mitochondria contact sites (EMCSs) are important for mitochondrial function. Here, we have identified a EMCS complex, comprising a family of uncharacterised mitochondrial outer- membrane proteins, TraB1, TraB2 and the ER protein, VAP27-1. In Arabidopsis, there are three TraB isoforms and the trab1a/trab2 double mutant exhibits abnormal mitochondrial morphology, strong starch accumulation and impaired energy metabolism, indicating that these proteins are essential for normal mitochondrial function. Moreover, TraB1 and TraB2 proteins also interact with ATG8 in order to regulate mitochondrial degradation (mitophagy). The turnover of depolarised mitochondria is significantly reduced in both trab1/trab2 and VAP27 mutants (vap27-1,3,4,6) under mitochondrial stress conditions, with an increased population of dysfunctional mitochondria present in the cytoplasm. Consequently, plant recovery after stress is significantly perturbed, suggesting that TraB1 regulated mitophagy and ER-mitochondrial interaction are two closely related processes. Taken together, we ascribe a dual role to TraB1 which is a component of the EMCS complex in eukaryotes, regulating both interaction of the mitochondria to the ER and mitophagy.

2022-08-30 | PXD036285 | Pride

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