Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/97403
Title: Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
Author: Le Roux, Anabel-Lise
Castro, Bruno
Garbacik, Erik T.
García-Parajó, Maria F.
Pons Vallès, Miquel
Keywords: Bicapes lipídiques
Proteïnes quinases
Transducció de senyal cel·lular
Membranes cel·lulars
Lipid bilayers
Protein kinases
Cellular signal transduction
Cell membranes
Issue Date: 8-Mar-2016
Publisher: Wiley-VCH
Abstract: 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.
Note: Reproducció del document publicat a: http://dx.doi.org/10.1002/slct.201600117
It is part of: ChemistrySelect, 2016, vol. 1, num. 4, p. 642-647
Related resource: http://dx.doi.org/10.1002/slct.201600117
URI: http://hdl.handle.net/2445/97403
ISSN: 2365-6549
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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