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Insulin-degrading enzyme regulates mRNA processing and interacts with the CCR4-NOT complex

ABSTRACT: Insulin-degrading enzyme regulates mRNA processing and interacts with the CCR4-NOT complex

PROVIDER: PRJNA1272523 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR33841695_1.fastq.gz	Fastqsanger.gz
	SRR33841695_2.fastq.gz	Fastqsanger.gz

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Insulin-degrading enzyme regulates mRNA processing and interacts with the CCR4-NOT complex

Project description:Insulin-degrading enzyme is a zinc metallo protease degrading low molecular weight substrates including insulin. Ubiquitous expression, high evolutionary conservation, upregulation of Ide in stress situations, and literature findings suggest a broader function of Ide in cell physiology and protein homeostasis that remains to be elucidated. We used proteomics and transcriptomics approaches searching for leads related to a broader role of Ide in protein homeostasis. We combined an analysis of the proteome and single-cell transcriptome of Ide+/+ and Ide-/- pancreatic islet cells with an examination of the interactome of human cytosolic Ide using proximity biotinylation. We observe an upregulation of pathways related to RNA processing, translation and splicing in Ide+/+ relative to Ide-/- islet cells. Corroborating these results and providing a potential mechanistic explanation, proximity biotinylation reveals interaction of Ide with several subunits of CCR4-NOT, a key mRNA deadenylase regulating gene expression "from birth to death". We propose a speculative model in which human and murine Ide and CCR4-NOT cooperate to control protein expression in proteotoxic and metabolic stress situations through cooperation between their deadenylase and protease functions.

2025-06-18 | GSE299071 | GEO

Insulin-degrading enzyme regulates mRNA processing and in-teracts with the CCR4-NOT transcription complex

Project description:Insulin-degrading enzyme is zinc metallo protease degrading low molecular weight substrates including insulin. Ubiquitous expression, high evolutionary conservation, upregulation of Ide in stress situations, and various literature findings suggest a broader function of Ide in cell physiology and protein homeostasis that remains to be elucidated. We used proteomics and transcriptomics approaches searching for leads related to a broader role of Ide in protein homeostasis. We combined an analysis of the proteome and single-cell transcriptome of Ide+/+ and Ide-/- pancreatic islet cells with an examination of the interactome of human cytosolic Ide using proximity biotinylation. We observe an upregulation of pathways related to RNA processing and translation in Ide+/+ relative to Ide-/- islet cells. Corroborating these results and providing a potential mechanistic explanation, proximity biotinylation reveals interaction of Ide with several subunits of CCR4-NOT, a key complex and mRNA deadenylase regulating protein expression "from birth to death". We propose a speculative model in which Ide and CCR4-NOT cooperate to control and limit protein expression in proteotoxic and met-abolic stress situations through cooperation between their deadenylase and protease functions.

2025-06-16 | PXD060228 | Pride

Effects of the insulin degrading enzyme silencing on the transcriptome of HepG2 cells

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Effects of the insulin degrading enzyme silencing on the transcriptome of HepG2 cells

Project description:Insulin degrading enzyme (IDE) is a major enzyme responsible for insulin degradation in the liver. The modulation of insulin degrading enzyme activity is hypothesized to be a link between T2DM and liver cancer. Results provide insight into role of IDE in proliferation and other cell functions. HepG2 cells were transfected with 96nM siRNA for IDE or AllStars Negative Control siRNA (Qiagen) using Lipofectamine 2000 (Invitrogen). 16 h after transfection, cells were treated with 10 nM insulin (Sigma Aldrich) or vehicle for 24 h in serum starvation condition. Total RNA was extracted. For each of the 4 conditions, 3 biological replicates were included.

2014-09-06 | E-GEOD-61142 | biostudies-arrayexpress

Insulin-Degrading Enzyme Regulates mRNA Processing and May Interact with the CCR4-NOT Complex.

Project description: Not available

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Expression data from Insulin Degrading Enzyme-Knocked Out hepatome human cells

Project description:Insulin-degrading enzyme (IDE) is a protein with proteolytic and non-proteolytic functions that regulates glucose homeostasis.We hypothesize that IDE deficiency alters glucagon signaling and thereby gluconeogenesis. To test this hypothesis we performed microarray studies in HepG2 cells with a complete deficiency of IDE gene. Results show that IDE deficiency led to upregulation of genes involved in cellular functions related to membranes, organelles and signaling receptors. We used microarrays to find genes whose expression is affected by the absence of IDE gene expression in hetapome human cells

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Expression data from Insulin Degrading Enzyme-Knocked Out hepatome human cells

Project description:Expression data from Insulin Degrading Enzyme-Knocked Out hepatome human cells

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Expression data from Insulin Degrading Enzyme-Knocked Down alpha pancreatic cells (mouse)

Project description:Insulin-degrading enzyme (IDE) is a protein with proteolytic and non-proteolytic functions that regulates primary cilium.We hypothesize that IDE deficiency alter expression of genes involved in the formation of the primary cilium . To test this hypothesis we performed microarray studies in mouse alphaTC1.9 cells with a partial deficiency of IDE gene. Results show that IDE knocdown led to regulation of genes involved in cellular functions related to primary cilium. We used microarrays to explore whether expression of genes related to cilliogenesis is affected by reduced expression of IDE gene in alpha pancreatic cells

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Expression data from Insulin Degrading Enzyme-Knocked Down alpha pancreatic cells (mouse)

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Insulin-Degrading Enzyme Interacts with Mitochondrial Ribosomes and Respiratory Chain Proteins.

Project description: Not available

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