Basonuclin-2 regulates extracellular matrix production and degradation

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dc.contributor.authorOrang, A.
dc.contributor.authorDredge, B.K.
dc.contributor.authorLiu, C.Y.
dc.contributor.authorBracken, J.M.
dc.contributor.authorChen, C.-H.
dc.contributor.authorSourdin, L.
dc.contributor.authorWhitfield, H.J.
dc.contributor.authorLumb, R.
dc.contributor.authorBoyle, S.T.
dc.contributor.authorDavis, M.J.
dc.contributor.authorSamuel, M.S.
dc.contributor.authorGregory, P.A.
dc.contributor.authorKhew-Goodall, Y.
dc.contributor.authorGoodall, G.J.
dc.contributor.authorPillman, K.A.
dc.contributor.authorBracken, C.P.
dc.date.issued2023
dc.descriptionPublished Online: 3 August, 2023
dc.description.abstractEpithelial-mesenchymal transition is essential for tissue patterning and organization. It involves both regulation of cell motility and alterations in the composition and organization of the ECM-a complex environment of proteoglycans and fibrous proteins essential for tissue homeostasis, signaling in response to chemical and biomechanical stimuli, and is often dysregulated under conditions such as cancer, fibrosis, and chronic wounds. Here, we demonstrate that basonuclin-2 (BNC2), a mesenchymal-expressed gene, that is, strongly associated with cancer and developmental defects across genome-wide association studies, is a novel regulator of ECM composition and degradation. We find that at endogenous levels, BNC2 controls the expression of specific collagens, matrix metalloproteases, and other matrisomal components in breast cancer cells, and in fibroblasts that are primarily responsible for the production and processing of the ECM within the tumour microenvironment. In so doing, BNC2 modulates the motile and invasive properties of cancers, which likely explains the association of high BNC2 expression with increasing cancer grade and poor patient prognosis.
dc.description.statementofresponsibilityAyla Orang, B Kate Dredge, Chi Yau Liu, Julie M Bracken, Chun-Hsien Chen, Laura Sourdin, Holly J Whitfield, Rachael Lumb, Sarah T Boyle, Melissa J Davis, Michael S Samuel, Philip A Gregory, Yeesim Khew-Goodall, Gregory J Goodall, Katherine A Pillman, Cameron P Bracken
dc.identifier.citationLife Science Alliance, 2023; 6(10):e202301984-1-e202301984-17
dc.identifier.doi10.26508/lsa.202301984
dc.identifier.issn2575-1077
dc.identifier.issn2575-1077
dc.identifier.orcidDredge, B.K. [0000-0002-6103-5165]
dc.identifier.orcidDavis, M.J. [0000-0003-4864-7033]
dc.identifier.orcidSamuel, M.S. [0000-0001-7880-6379]
dc.identifier.orcidGregory, P.A. [0000-0002-0999-0632]
dc.identifier.orcidKhew-Goodall, Y. [0000-0002-0473-5392]
dc.identifier.orcidGoodall, G.J. [0000-0003-1294-0692]
dc.identifier.orcidPillman, K.A. [0000-0002-5869-889X]
dc.identifier.urihttps://hdl.handle.net/2440/141472
dc.language.isoen
dc.publisherLife Science Alliance LLC
dc.relation.granthttp://purl.org/au-research/grants/arc/FT190100544
dc.rights© 2023 Orang et al. License: This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).
dc.source.urihttps://doi.org/10.26508/lsa.202301984
dc.subjectEpithelial-Mesenchymal Transition
dc.subject.meshHumans
dc.subject.meshGenome-Wide Association Study
dc.subject.meshExtracellular Matrix
dc.subject.meshNeoplasms
dc.subject.meshCollagen
dc.subject.meshEpithelial-Mesenchymal Transition
dc.subject.meshTumor Microenvironment
dc.subject.meshDNA-Binding Proteins
dc.titleBasonuclin-2 regulates extracellular matrix production and degradation
dc.typeJournal article
pubs.publication-statusPublished

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