{"id":403,"date":"2021-03-15T10:13:34","date_gmt":"2021-03-15T10:13:34","guid":{"rendered":"https:\/\/website.prod.unilu.spikeseed.cloud\/fstm-fr\/news\/better-understanding-breast-cancer\/"},"modified":"2021-03-15T10:13:34","modified_gmt":"2021-03-15T10:13:34","slug":"better-understanding-breast-cancer","status":"publish","type":"news","link":"https:\/\/www.uni.lu\/fstm-fr\/news\/better-understanding-breast-cancer\/","title":{"rendered":"Better understanding breast cancer"},"content":{"rendered":"

Researchers from the University of Luxembourg have demonstrated that Ser5 phosphorylation of the actin-bundling protein L-plastin increases breast cancer cell invasiveness. Their findings have been published in the renowned open access journal \u201cCell Communication and Signaling\u201d.<\/p>

Role of L-plastin<\/strong><\/p>

Metastasis is the predominant cause for cancer morbidity and mortality accounting for approximatively 90% of cancer deaths. The actin-bundling protein L-plastin has been proposed as a metastatic marker and phosphorylation on its residue Ser5 is known to increase its actin-bundling activity. \u201cWe recently showed that activation of the ERK\/MAPK signalling pathway leads to L-plastin Ser5 phosphorylation and that the downstream kinases RSK1 and RSK2 are able to directly phosphorylate Ser5. Here we investigate the involvement of the PI3K pathway in L-plastin Ser5 phosphorylation and the functional effect of this phosphorylation event in breast cancer cells\u201d, explains Elisabeth Schaffner\u2011Reckinger<\/a>, research scientist at the Department of Life Sciences and Medicine (DLSM)<\/a> at the University of Luxembourg and principal investigator of the study.<\/p>

Research via modelling and experiment<\/strong><\/p>

\u201cTo unravel the signal transduction network upstream of L-plastin Ser5 phosphorylation, we performed computational modelling based on immunoblot analysis data, followed by experimental validation through inhibition\/ overexpression studies and in vitro kinase assays. To assess the functional impact of L-plastin expression\/Ser5 phosphorylation in breast cancer cells, we either silenced L-plastin in cell lines initially expressing endogenous L-plastin or neoexpressed L-plastin wild type and phosphovariants in cell lines devoid of endogenous L-plastin. The established cell lines were used for cell biology experiments and confocal microscopy analysis. Our modelling approach revealed that, in addition to the ERK\/MAPK pathway and depending on the cellular context, the PI3K pathway contributes to L-plastin Ser5 phosphorylation through its downstream kinase SGK3.\u201d, comments Raquel Martinez Machado<\/a>, postdoctoral researcher who performed most of the experimental work of the study.<\/p>

L-plastin is proposed here as a potential target for therapeutic approaches that are aimed at blocking dysregulated signalling outcome of both pathways and, thus, at impairing cancer cell invasion and metastasis formation.<\/p>

Article: \u00ab\u00a0L-plastin Ser5 phosphorylation is modulated by the PI3K\/SGK pathway and promotes breast cancer cell invasiveness<\/a>\u00ab\u00a0, Cell Communication and Signaling, February 2021<\/p><\/div><\/section>","protected":false},"excerpt":{"rendered":"

Researchers from the University of Luxembourg have demonstrated that Ser5 phosphorylation of the actin-bundling protein L-plastin increases breast cancer cell invasiveness. 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