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Endoplasmic Reticulum (ER) Chaperones Are Effector Genes Mediating Long-Term Memory Consolidation

ABSTRACT: Endoplasmic Reticulum (ER) Chaperones Are Effector Genes Mediating Long-Term Memory Consolidation

PROVIDER: PRJNA704968 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR13785841_1.fastq.gz	Fastqsanger.gz
	SRR13785841_2.fastq.gz	Fastqsanger.gz
	SRR13785842_1.fastq.gz	Fastqsanger.gz
	SRR13785842_2.fastq.gz	Fastqsanger.gz
	SRR13785843_1.fastq.gz	Fastqsanger.gz

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Endoplasmic Reticulum (ER) Chaperones Are Effector Genes Mediating Long-Term Memory Consolidation

Project description:Purpose: We investigated Nr4a effector genes following a hippocampus dependent learning task using a dominant mouse model of Nr4a. Method: We performed total RNA sequencing after training for hippocampus-dependent memory from Nr4ADN and control littermates Results: Using an unbiased analysis of gene expression after training for hippocampus-dependent memory, we found that Nr4a transcription factors regulate expression of specific effector genes encoding endoplasmic reticulum (ER) chaperones that drive protein folding, enabling membrane proteins to more efficiently traffic to the cell surface. Conclusion: This study identified the effector genes of Nr4a transcription factors involved in learning and memory.

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Membrane association and activity of rough endoplasmic reticulum associated RISC requires farnesylated chaperones

Project description:Membrane association and activity of rough endoplasmic reticulum associated RISC requires farnesylated chaperones

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Mutant PDIA3 causes neurodevelopmental impairment by disturbing endoplasmic reticulum proteostasis

Project description:Identification of a disease gene enables the elucidation of the gene function in biological networks. Here we report homozygous c.170G>A (p.Cys57Tyr or C57Y) in protein disulfide isomerase A3 (PDIA3) causing syndromic intellectual disability. PDIA3 catalyzes the formation of disulfide bonds in the endoplasmic reticulum. Experiments in zebrafish embryos showed that PDIA3C57Y is pathogenic, causing developmental problems such as axonal disorganization and skeleton abnormalities. In mammalian models, expression of PDIA3C57Y inhibited axonal growth and impaired synaptic plasticity and memory consolidation. Proteomic and functional analysis revealed that PDIA3C57Y leads to dysregulation of cell adhesion and actin cytoskeleton dynamics associated with altered integrin biogenesis. These alterations were correlated with low catalytic activity of PDIA3C57Y, which also forms disulfide-crosslinked aggregates that abnormally interact with chaperones in the endoplasmic reticulum. This study shows that the disturbance of the proteostasis network in intellectual disability cases adversely impacts cellular connectivity and neuronal function, constituting a pathogenic pathway to neurodevelopmental impairment.

2021-11-25 | PXD026507 | Pride

Ribosome footprinting in the cytosol and endoplasmic reticulum

Project description:In eukaryotic cells, the spatial regulation of protein expression is frequently conferred through the coupling of mRNA localization and the local control of translation. mRNA localization to the endoplasmic reticulum (ER) is a prominent example of such regulation and serves a ubiquitous role in segregating the synthesis of secretory and integral membrane proteins to the ER. Recent genomic and biochemical studies have now expanded this view to suggest a role for the ER in global protein synthesis. We have utilized cell fractionation and ribosome profiling to obtain a genomic survey of the subcellular organization of mRNA translation and report that ribosomal loading of mRNAs, a proxy for mRNA translation, is biased to the ER. Notably, ER-associated mRNAs encoding both cytosolic and topogenic signal-encoding proteins display similar ribosome loading densities, suggesting that ER-associated ribosomes serve a global role in mRNA translation. We propose that the partitioning of mRNAs and their translation between the cytosol and ER compartments may represent a novel mechanism for the post-transcriptional regulation of gene expression. HEK293 cells were fractionated between the cytosol and endoplasmic reticulum. Within each fraction, ribosome footprints were generated and sequenced. In parallel, total mRNA was sequenced.

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Tunicamycin-induced Endoplasmic Reticulum-Quality Control Pathway and Endoplasmic Reticulum-Associated Degradation Mechanism in the diatom Phaeodactylum tricornutum

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The SND proteins constitute an alternative targeting route to the endoplasmic reticulum

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.

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Mutant p53 promotes tumor progression by the endoplasmic reticulum UDPase ENTPD5

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