Publication:
A homozygous pathogenic missense variant broadens the phenotypic and mutational spectrum of CREB3L1-related osteogenesis imperfecta

dc.contributor.coauthorGuillemyn, Brecht
dc.contributor.coauthorDemuynck, Lynn
dc.contributor.coauthorSips, Patrick
dc.contributor.coauthorDe Paepe, Anne
dc.contributor.coauthorSyx, Delfien
dc.contributor.coauthorCoucke, Paul J.
dc.contributor.coauthorMalfait, Fransiska
dc.contributor.coauthorSymoens, Sofie
dc.contributor.departmentSchool of Medicine
dc.contributor.kuauthorKayserili, Hülya
dc.contributor.schoolcollegeinstituteSCHOOL OF MEDICINE
dc.date.accessioned2024-11-10T00:12:25Z
dc.date.issued2019
dc.description.abstractThe cyclic adenosine monophosphate responsive element binding protein 3-like 1 (CREB3L1) gene codes for the endoplasmic reticulum stress transducer old astrocyte specifically induced substance (OASIS), which has an important role in osteoblast differentiation during bone development. Deficiency of OASIS is linked to a severe form of autosomal recessive osteogenesis imperfecta (OI), but only few patients have been reported. We identified the first homozygous pathogenic missense variant [p.(Ala304Val)] in a patient with lethal OI, which is located within the highly conserved basic leucine zipper domain, four amino acids upstream of the DNA binding domain. In vitro structural modeling and luciferase assays demonstrate that this missense variant affects a critical residue in this functional domain, thereby decreasing the type I collagen transcriptional binding ability. In addition, overexpression of the mutant OASIS protein leads to decreased transcription of the SEC23A and SEC24D genes, which code for components of the coat protein complex type II (COPII), and aberrant OASIS signaling also results in decreased protein levels of SEC24D. Our findings therefore provide additional proof of the potential involvement of the COPII secretory complex in the context of bone-associated disease.
dc.description.indexedbyWOS
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.issue11
dc.description.openaccessYES
dc.description.publisherscopeInternational
dc.description.sponsoredbyTubitakEuN/A
dc.description.sponsorshipResearch Foundation Flanders [12Q5917N, 1842318N]
dc.description.sponsorshipGhent University [08/01M01108]
dc.description.sponsorshipEuropean Union [794365] Research Foundation Flanders (12Q5917N to D.S., 1842318N to F.M.)
dc.description.sponsorshipGhent University (08/01M01108 to A.D.P.)
dc.description.sponsorshipEuropean Union's Horizon 2020 research and innovation program Marie SklodoWSKa-Curie (794365 to P.S.).
dc.description.volume28
dc.identifier.doi10.1093/hmg/ddz017
dc.identifier.eissn1460-2083
dc.identifier.issn0964-6906
dc.identifier.quartileQ1
dc.identifier.scopus2-s2.0-85066868311
dc.identifier.urihttps://doi.org/10.1093/hmg/ddz017
dc.identifier.urihttps://hdl.handle.net/20.500.14288/17657
dc.identifier.wos475889300004
dc.keywordsReticulum stress-response
dc.keywordsProlyl 3-hydroxylation
dc.keywordsBruck-syndrome
dc.keywordsOasis
dc.language.isoeng
dc.publisherOxford Univ Press
dc.relation.ispartofHuman Molecular Genetics
dc.subjectBiochemistry
dc.subjectMolecular biology
dc.subjectGenetics
dc.subjectHeredity
dc.titleA homozygous pathogenic missense variant broadens the phenotypic and mutational spectrum of CREB3L1-related osteogenesis imperfecta
dc.typeJournal Article
dspace.entity.typePublication
local.contributor.kuauthorKayserili, Hülya
local.publication.orgunit1SCHOOL OF MEDICINE
local.publication.orgunit2School of Medicine
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relation.isParentOrgUnitOfPublication17f2dc8e-6e54-4fa8-b5e0-d6415123a93e
relation.isParentOrgUnitOfPublication.latestForDiscovery17f2dc8e-6e54-4fa8-b5e0-d6415123a93e

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