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Proteasome Stress in Skeletal Muscle Mounts a Long-Range Protective Response that Delays Retinal and Brain Aging [Drosophila]

ABSTRACT: Proteasome Stress in Skeletal Muscle Mounts a Long-Range Protective Response that Delays Retinal and Brain Aging [Drosophila]

PROVIDER: PRJNA630174 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11684144_1.fastq.gz	Fastqsanger.gz
	SRR11684144_2.fastq.gz	Fastqsanger.gz
	SRR11684145_1.fastq.gz	Fastqsanger.gz
	SRR11684145_2.fastq.gz	Fastqsanger.gz
	SRR11684146_1.fastq.gz	Fastqsanger.gz

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Proteasome Stress in Skeletal Muscle Mounts a Long-Range Protective Response that Delays Retinal and Brain Aging

Project description:Proteasome Stress in Skeletal Muscle Mounts a Long-Range Protective Response that Delays Retinal and Brain Aging

| PRJNA630171 | ENA

Proteasome Stress in Skeletal Muscle Mounts a Long-Range Protective Response that Delays Retinal and Brain Aging [Human]

Project description:Proteasome Stress in Skeletal Muscle Mounts a Long-Range Protective Response that Delays Retinal and Brain Aging [Human]

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Proteasome Stress in Skeletal Muscle Mounts a Long-Range Protective Response that Delays Retinal and Brain Aging [Drosophila]

Project description:The proteasome maintains protein quality during aging and disease. Challenges to proteasome function can be compensated by local proteasome stress responses. However, whereas proteasome stress is also sensed systemically is unknown. In Drosophila , we find that proteasome stress in skeletal muscle non-autonomously promotes the degradation of proteasome substrates in distant tissues during aging. Several muscle-secreted factors (myokines) are upregulated by proteasomal stress via C/EBP transcription factors, including the amylase Amyrel, which increases the circulating levels of the disaccharide maltose. Muscle-specific Amyrel overexpression promotes the degradation of proteasome substrates in the aging brain and retina via the transcriptional induction of chaperones and proteases. Conversely, RNAi for maltose transporters worsens proteostasis and reduces the expression of Amyrel-induced genes in the brain. Moreover, maltose preserves protein quality in cell culture and human cortical brain organoids challenged by thermal stress. Thus, proteasome stress in skeletal muscle mounts a systemic adaptive response via amylase/maltose signaling.

2021-02-12 | GSE149798 | GEO

Proteasome Stress in Skeletal Muscle Mounts a Long-Range Protective Response that Delays Retinal and Brain Aging [Human]

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Proteasome stress in skeletal muscle mounts a long-range protective response that delays retinal and brain aging.

Project description:Neurodegeneration in the central nervous system (CNS) is a defining feature of organismal aging that is influenced by peripheral tissues. Clinical observations indicate that skeletal muscle influences CNS aging, but the underlying muscle-to-brain signaling remains unexplored. In Drosophila, we find that moderate perturbation of the proteasome in skeletal muscle induces compensatory preservation of CNS proteostasis during aging. Such long-range stress signaling depends on muscle-secreted Amyrel amylase. Mimicking stress-induced Amyrel upregulation in muscle reduces age-related accumulation of poly-ubiquitinated proteins in the brain and retina via chaperones. Preservation of proteostasis stems from the disaccharide maltose, which is produced via Amyrel amylase activity. Correspondingly, RNAi for SLC45 maltose transporters reduces expression of Amyrel-induced chaperones and worsens brain proteostasis during aging. Moreover, maltose preserves proteostasis and neuronal activity in human brain organoids challenged by thermal stress. Thus, proteasome stress in skeletal muscle hinders retinal and brain aging by mounting an adaptive response via amylase/maltose.

| S-EPMC8172468 | biostudies-literature

Proteasome Stress in Skeletal Muscle Mounts a Long-Range Protective Response that Delays Retinal and Brain Aging

Project description:This SuperSeries is composed of the SubSeries listed below.

2021-02-12 | GSE149799 | GEO

GLA and profiling of proteasome, Spt23 and Mga2

Project description:The proteasome can regulate transcription through proteolytic processing of transcription factors and via gene locus binding, but few targets of proteasomal regulation have been identified. Using genome-wide location analysis and transcriptional profiling in Saccharomyces cerevisiae, we have established which genes are bound and regulated by the proteasome, and by Spt23 and Mga2, transcription factors activated by the proteasome. We observed proteasome association with gene sets that are highly transcribed, controlled by the mating-type loci, and involved in lipid metabolism. At ribosomal protein genes, proteasome and RNA polymerase II binding was enriched in a proteasome mutant, indicating a role for the proteasome in dissociating elongation complexes. The genomic occupancies of Spt23 and Mga2 overlapped significantly with the genes bound by the proteasome. Finally, the proteasome acts in two distinct ways, one dependent and one independent of Spt23/Mga2 cleavage, providing evidence for cooperative gene regulation by the proteasome and its substrates. Keywords: ChIP-chip; genetic modification transcriptional profiling Six genomic localization analysis (GLA, ChIP2) experiments are represented by 18 samples. Six transcriptional profiling experiments (prof) are also represented. Experiments were generally done in triplicate, with fluors swapped on the third replicate.

2006-02-28 | E-GEOD-4272 | biostudies-arrayexpress

GLA and profiling of proteasome, Spt23 and Mga2

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Cellular response to proteasome inhibition by Bortezomib

Project description:Analysis of the coordinated transcriptional reponse to proteasome inhibition mRNA profiles of NIH3T3 cells which stably expressing DD-sfGFP were generated by deep sequencing using Illumina HiSeq. The samples were collected from indicated timepoints after exposed to proteasome inhibition by Bortezomib.

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Ubiquitin proteasome expression in Mulitple Myeloma cell lines

Project description:The ubiquitin proteasome system plays an important role in the pathophysiology of Multiple Myeloma, highlighted by the unique success of proteasome inhibitors in this malignancy. Using topic-defined microarrays we have looked at expression of ubiquitin proteasome system genes in 2 multiple myeloma cell lines and normal bone marrow samples.

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