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bioRxiv · 10.1101/2021.04.15.439909

XBP1s-Mediated Endoplasmic Reticulum Proteostasis Network Enhancement Can Selectively Improve Folding and Secretion of an Osteogenesis Imperfecta-Causing Collagen-I Variant

Abstract

Osteogenesis imperfecta (OI) is typically caused by autosomal dominant mutations in genes encoding collagen type-I, most commonly resulting in Gly[->]Ser triple-helical domain substitutions that disrupt collagen folding and/or stability. Here, we test the hypothesis that upregulating the endoplasmic reticulum (ER) proteo-stasis network via the unfolded protein response (UPR) can improve the folding and secretion of the clinically severe, prototypical OI-causing COL1A1 p.G425S collagen-1(I) variant. We first show that small molecules that activate the entire UPR by causing global ER protein misfolding stress severely ablate collagen-I secretion from both G425S Col1(I)- and wild-type (WT) Col1(I)-expressing primary fibroblasts. In contrast, stress-independent, specific induction of just the UPRs XBP1s transcriptional response can enhance collagen-I secretion from G425S Col1(I) patient primary fibroblasts up to ~300% of basal levels. Notably, the effect is selective - collagen-I secretion from WT Col1(I)-expressing healthy donor primary fibroblasts is unaltered by XBP1s. XBP1s pathway activation appears to post-translationally enhance the folding/assembly and secretion of G425S Col1(I), as only modest impacts on collagen-I transcription or synthesis are observed. Consistent with this notion, we find that the stable, triple-helical collagen-I secreted by XBP1s-activated G425S 1(I) patient fibroblasts includes a higher proportion of the mutant 1(I) polypeptide than the collagen-I secreted under basal ER proteostasis conditions. We note that consistent reproducibility of these results is dependent on as yet unascertained experimental variables. Still, these promising observations suggest the potential for ER proteo-stasis network modulation to improve mutant collagen proteostasis in the collagenopathies, motivating further investigation of the effects generality, underlying mechanism, and potential therapeutic benefits.

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BibTeXRIS

DiChiara, A. S., Doan, N.-D., Bikovtseva, A., Rowley, L., Butty, V., Weis, M., Eyre, D., Lamande, S., Bateman, J. F., Shoulders, M. D.. 2021-04-16. XBP1s-Mediated Endoplasmic Reticulum Proteostasis Network Enhancement Can Selectively Improve Folding and Secretion of an Osteogenesis Imperfecta-Causing Collagen-I Variant. https://doi.org/10.1101/2021.04.15.439909

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