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ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (P5 parietal bone)

ABSTRACT: We used single cell RNA sequencing (scRNA-seq) to identify parietal osteoblast cell stress response pathway to misfolding of type I procollagen with Gly610->Cys substitution in the triple helical region of alpha2(I) chain.

ORGANISM(S): Mus musculus

PROVIDER: GSE210519 | GEO | 2022/08/07

REPOSITORIES: GEO

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ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (primary cells)

Project description:We used bulk RNA sequencing (bulk RNAseq) in primary osteoblast cultures to validate scRNASeq and srRNASeq findings on osteoblast cell stress response pathway to misfolding of type I procollagen with Gly610->Cys substitution in the triple helical region of alpha2(I) chain.

2022-08-12 | GSE210796 | GEO

ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (E18.5 femur and tibia)

Project description:We used single cell RNA sequencing (scRNA-seq) to identify femur and tibia osteoblast cell stress response pathway to misfolding of type I procollagen with Gly610->Cys substitution in the triple helical region of alpha2(I) chain.

2022-08-07 | GSE210511 | GEO

ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (proximal tibia srRNASeq)

Project description:We used spatially resolved RNA sequencing (srRNA-seq) to identify trabecular osteoblast cell stress response pathway to misfolding of type I procollagen with Gly610->Cys substitution in the triple helical region of alpha2(I) chain (trabecular region of proximal tibia adjacent to the growth plate).

2022-08-08 | GSE210637 | GEO

ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (P5 parietal bone)

Project description:ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (P5 parietal bone)

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ER, Mitochondria, and ISR Regulation by mt-HSP70 and ATF5 upon Procollagen Misfolding in Osteoblasts.

Project description:Cellular response to protein misfolding underlies multiple diseases. Collagens are the most abundant vertebrate proteins, yet little is known about cellular response to misfolding of their procollagen precursors. Osteoblasts (OBs)-the cells that make bone-produce so much procollagen that it accounts for up to 40% of mRNAs in the cell, which is why bone bears the brunt of mutations causing procollagen misfolding in osteogenesis imperfecta (OI). The present study of a G610C mouse model of OI by multiple transcriptomic techniques provides first solid clues to how OBs respond to misfolded procollagen accumulation in the endoplasmic reticulum (ER) and how this response affects OB function. Surprisingly, misfolded procollagen escapes the quality control in the ER lumen and indirectly triggers the integrated stress response (ISR) through other cell compartments. In G610C OBs, the ISR is regulated by mitochondrial HSP70 (mt-HSP70) and ATF5 instead of their BIP and ATF4 paralogues, which normally activate and regulate ISR to secretory protein misfolding in the ER. The involvement of mt-HSP70 and ATF5 together with other transcriptomic findings suggest that mitochondria might initiate the ISR upon disruption of ER-mitochondria connections or might respond to the ISR activated by a yet unknown sensor.

| S-EPMC9561870 | biostudies-literature

ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (primary cells)

Project description:ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (primary cells)

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ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (proximal tibia srRNASeq)

Project description:ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (proximal tibia srRNASeq)

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ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (E18.5 femur and tibia)

Project description:ER, mitochondria and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding (E18.5 femur and tibia)

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Redox control of the cAMP/PKA pathway during protein misfolding stress

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Cytoplasmic protein misfolding titrates Hsp70 to activate nuclear Hsf1.

Project description:Hsf1 is an ancient transcription factor that responds to protein folding stress by inducing the heat-shock response (HSR) that restore perturbed proteostasis. Hsp70 chaperones negatively regulate the activity of Hsf1 via stress-responsive mechanisms that are poorly understood. Here, we have reconstituted budding yeast Hsf1-Hsp70 activation complexes and find that surplus Hsp70 inhibits Hsf1 DNA-binding activity. Hsp70 binds Hsf1 via its canonical substrate binding domain and Hsp70 regulates Hsf1 DNA-binding activity. During heat shock, Hsp70 is out-titrated by misfolded proteins derived from ongoing translation in the cytosol. Pushing the boundaries of the regulatory system unveils a genetic hyperstress program that is triggered by proteostasis collapse and involves an enlarged Hsf1 regulon. The findings demonstrate how an apparently simple chaperone-titration mechanism produces diversified transcriptional output in response to distinct stress loads.

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