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 |
URI: | http://hdl.handle.net/2445/97403 |
Related resource: | http://dx.doi.org/10.1002/slct.201600117 |
ISSN: | 2365-6549 |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
660240.pdf | 1.49 MB | Adobe PDF | View/Open |
This item is licensed under a Creative Commons License