The oncogenic tyrosine kinase Lyn impairs the pro-apoptotic function of Bim View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-04

AUTHORS

Lazaro E. Aira, Elodie Villa, Pascal Colosetti, Parvati Gamas, Laurie Signetti, Sandrine Obba, Emma Proics, Fabien Gautier, Béatrice Bailly-Maitre, Arnaud Jacquel, Guillaume Robert, Frédéric Luciano, Philippe P. Juin, Jean-Ehrland Ricci, Patrick Auberger, Sandrine Marchetti

ABSTRACT

Phosphorylation of Ser/Thr residues is a well-established modulating mechanism of the pro-apoptotic function of the BH3-only protein Bim. However, nothing is known about the putative tyrosine phosphorylation of this Bcl-2 family member and its potential impact on Bim function and subsequent Bax/Bak-mediated cytochrome c release and apoptosis. As we have previously shown that the tyrosine kinase Lyn could behave as an anti-apoptotic molecule, we investigated whether this Src family member could directly regulate the pro-apoptotic function of Bim. In the present study, we show that Bim is phosphorylated onto tyrosine residues 92 and 161 by Lyn, which results in an inhibition of its pro-apoptotic function. Mechanistically, we show that Lyn-dependent tyrosine phosphorylation of Bim increases its interaction with anti-apoptotic members such as Bcl-xL, therefore limiting mitochondrial outer membrane permeabilization and subsequent apoptosis. Collectively, our data uncover one molecular mechanism through which the oncogenic tyrosine kinase Lyn negatively regulates the mitochondrial apoptotic pathway, which may contribute to the transformation and/or the chemotherapeutic resistance of cancer cells. More... »

PAGES

2122-2136

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41388-017-0112-0

DOI

http://dx.doi.org/10.1038/s41388-017-0112-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1100745399

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29391601


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