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dc.contributor.authorMohamed, Raafat
dc.contributor.authorShajimoon, Aravindra
dc.contributor.authorAfroz, Rizwana
dc.contributor.authorGabr, Mai
dc.contributor.authorThomas, Walter G
dc.contributor.authorLittle, Peter J
dc.contributor.authorKamato, Danielle
dc.date.accessioned2022-02-18T00:52:41Z
dc.date.available2022-02-18T00:52:41Z
dc.date.issued2021
dc.identifier.issn1742-464X
dc.identifier.doi10.1111/febs.16297
dc.identifier.urihttp://hdl.handle.net/10072/412450
dc.description.abstractTransforming growth factor (TGF)-β signalling commences with the engagement of TGF-β ligand to cell surface TGF-β receptors (TGFBR) stimulating Smad2 carboxyl-terminal phosphorylation (phospho-Smad2C) and downstream biological responses. In several cell models, G protein-coupled receptors (GPCRs) transactivate the TGF-β receptors type-1 (TGFBR1) leading to phospho-Smad2C, however, we have recently published that in keratinocytes thrombin did not transactivate the TGFBR1. The bulk of TGFBRs reside in the cytosol and in response to protein kinase B (Akt phosphorylation) can translocate to the cell surface increasing the cell's responsiveness to TGF-β. In this study, we investigate the role of Akt in GPCR transactivation of the TGFBR1. We demonstrate that angiotensin II and thrombin do not phosphorylate Smad2C in human vascular smooth muscle cells and in keratinocytes respectively. We used Akt agonist, SC79 to sensitise the cells to Akt and observed that Ang II and thrombin phosphorylate Smad2C via Akt/AS160-dependent pathways. We show that SC79 rapidly translocates TGFBRs to the cell surface thus increasing the cell's response to the GPCR agonist. These findings highlight novel mechanistic insight for the role of Akt in GPCR transactivation of the TGFBR1. k
dc.description.peerreviewedYes
dc.languageen
dc.publisherWiley
dc.relation.ispartofjournalThe FEBS Journal
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchMedical biochemistry and metabolomics
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode3205
dc.subject.fieldofresearchcode3404
dc.titleAkt acts as a switch for GPCR transactivation of the TGF‐β receptor type 1
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationMohamed, R; Shajimoon, A; Afroz, R; Gabr, M; Thomas, WG; Little, PJ; Kamato, D, Akt acts as a switch for GPCR transactivation of the TGF‐β receptor type 1, The FEBS Journal
dc.date.updated2022-02-17T05:15:42Z
gro.description.notepublicThis publication has been entered as an advanced online version in Griffith Research Online.
gro.hasfulltextNo Full Text
gro.griffith.authorAfroz, Rizwana
gro.griffith.authorKamato, Danielle


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