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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/97403
Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
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The 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.
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LE ROUX, Anabel-Lise, et al. Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers. ChemistrySelect. 2016. Vol. 1, num. 4, pags. 642-647. ISSN 2365-6549. [consulted: 11 of June of 2026]. Available at: https://hdl.handle.net/2445/97403