Le Roux, Anabel-LiseCastro, BrunoGarbacik, Erik T.García-Parajó, Maria F.Pons Vallès, Miquel2016-04-142016-03-082365-6549https://hdl.handle.net/2445/97403The proto-oncogene tyrosine-protein kinase Src is a key ele- ment of signaling cascades involved in the invasive and meta- stasis-forming capacity of cancer cells. While membrane ty- rosine-kinase receptors are known to dimerize, Src is classified as a non-receptor kinase and assumed to remain always mono- meric. Here we demonstrate the formation of stable dimers by the first domains of myristoylated Src previously shown to be sufficient for Src trafficking. Src dimers fused to green fluo- rescent protein (GFP) on supported lipid bilayers were identi- fied using single-molecule photobleaching experiments. Com- petition with a protein containing only native Src domains without GFP confirms that dimerization is a previously over- looked intrinsic property of Src. Dimerization is concomitant to membrane binding by the myristoylated forms of Src and may constitute a new regulation layer for the Src oncogene.6 p.application/pdfengcc by-nc (c) Le Roux et al., 2016http://creativecommons.org/licenses/by-nd/3.0/es/Bicapes lipídiquesProteïnes quinasesTransducció de senyal cel·lularMembranes cel·lularsLipid bilayersProtein kinasesCellular signal transductionCell membranesinfo:eu-repo/semantics/article6602402016-04-14info:eu-repo/semantics/openAccess