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Article: Inorganic polyphosphate controls cyclophilin B‐mediated collagen folding in osteoblast‐like cells

TitleInorganic polyphosphate controls cyclophilin B‐mediated collagen folding in osteoblast‐like cells
Authors
Keywordscollagen folding
cyclophilin B
osteoblast‐like cells
polyphosphate
SaOS‐2 cells
Issue Date2020
PublisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1742-4658
Citation
The FEBS Journal, 2020, v. 287 n. 20, p. 4500-4524 How to Cite?
AbstractEvidence is emerging that inorganic polyphosphate (polyP) is a fundamental molecule involved in a wide range of biological processes. In higher eukaryotes, polyP is abundant in osteoblasts but questions remain as to its functions. Here, we find that polyP is particularly enriched in endoplasmic reticulum (ER) where it colocalizes with cyclophilin B (CypB) using osteoblastic SaOS‐2 model cell line. PolyP binds directly and specifically to CypB, inhibiting its peptidyl‐prolyl cis‐trans isomerase activity which is critical for collagen folding. PolyP sequestration by spermine and ER‐specific polyP reduction by polyphosphatase expression in cells reduced collagen misfolding and confirmed that endogenous polyP acts as a molecular control of CypB‐mediated collagen folding. We propose that polyP is a previously unrecognized critical regulator of protein homeostasis in ER.
Persistent Identifierhttp://hdl.handle.net/10722/290269
ISSN
2023 Impact Factor: 5.5
2023 SCImago Journal Rankings: 2.003
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorKHONG, ML-
dc.contributor.authorLi, L-
dc.contributor.authorSolesio, ME-
dc.contributor.authorPavlov, EV-
dc.contributor.authorTanner, JA-
dc.date.accessioned2020-10-22T08:24:22Z-
dc.date.available2020-10-22T08:24:22Z-
dc.date.issued2020-
dc.identifier.citationThe FEBS Journal, 2020, v. 287 n. 20, p. 4500-4524-
dc.identifier.issn1742-464X-
dc.identifier.urihttp://hdl.handle.net/10722/290269-
dc.description.abstractEvidence is emerging that inorganic polyphosphate (polyP) is a fundamental molecule involved in a wide range of biological processes. In higher eukaryotes, polyP is abundant in osteoblasts but questions remain as to its functions. Here, we find that polyP is particularly enriched in endoplasmic reticulum (ER) where it colocalizes with cyclophilin B (CypB) using osteoblastic SaOS‐2 model cell line. PolyP binds directly and specifically to CypB, inhibiting its peptidyl‐prolyl cis‐trans isomerase activity which is critical for collagen folding. PolyP sequestration by spermine and ER‐specific polyP reduction by polyphosphatase expression in cells reduced collagen misfolding and confirmed that endogenous polyP acts as a molecular control of CypB‐mediated collagen folding. We propose that polyP is a previously unrecognized critical regulator of protein homeostasis in ER.-
dc.languageeng-
dc.publisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1742-4658-
dc.relation.ispartofThe FEBS Journal-
dc.rightsPreprint This is the pre-peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. Postprint This is the peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.-
dc.subjectcollagen folding-
dc.subjectcyclophilin B-
dc.subjectosteoblast‐like cells-
dc.subjectpolyphosphate-
dc.subjectSaOS‐2 cells-
dc.titleInorganic polyphosphate controls cyclophilin B‐mediated collagen folding in osteoblast‐like cells-
dc.typeArticle-
dc.identifier.emailTanner, JA: jatanner@hkucc.hku.hk-
dc.identifier.authorityTanner, JA=rp00495-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1111/febs.15249-
dc.identifier.pmid32056376-
dc.identifier.pmcidPMC7423684-
dc.identifier.scopuseid_2-s2.0-85082326683-
dc.identifier.hkuros316975-
dc.identifier.volume287-
dc.identifier.issue20-
dc.identifier.spage4500-
dc.identifier.epage4524-
dc.identifier.isiWOS:000561927000001-
dc.publisher.placeUnited Kingdom-
dc.identifier.issnl1742-464X-

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