ArticleCell communication and signaling : CCS2018
Ras enhances TGF-β signaling by decreasing cellular protein levels of its type II receptor negative regulator SPSB1.
Article in Cell communication and signaling : CCS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundTransformation by oncogene Ras overcomes TGF-β mediated growth inhibition in epithelial cells. However, it cooperates with each other to mediate epithelial to mesenchymal transition (EMT). The mechanism of how these two pathways interact with each other is controversial.
methodsMolecular techniques were used to engineer expression plasmids for Ras, SPRY, TGF-β receptors, type I and II and ubiquitin. Immunoprecipitation and western blots were employed to determine protein-protein interactions, preotein levels, protein phosphorylation while immunofluorecesent staining for molecular co-localization. TGF-β signalling activities is also determined by its luciferase reporter assay. Trans-well assays were used to measure cell migration and invasion.
resultsRas interacts with the SPSB1's SPRY domain to enhance TGF-β signaling. Ras interacts and colocalizes with the TGF-β type II receptor's (TβRII) negative regulator SPSB1 on the cell membrane, consequently promoting SPSB1 protein degradation via enhanced mono- and di-ubiquitination. Reduced SPSB1 levels result in the stablization of TβRII, in turn the increase of receptor levels significantly enhance Smad2/3 phosphorylation and signaling. Importantly, forced expression of SPSB1 in Ras transformed cells suppresses TGF-β signaling and its mediated migration and invasion.
conclusionRas positively cooperates with TGF-β signaling by reducing the cellular protein levels of TβRII negative regualtor SPSB1.
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