Title:
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Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
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Author:
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Le Roux, Anabel-Lise; Castro, Bruno; Garbacik, Erik T.; García-Parajó, Maria F.; Pons Vallès, Miquel
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Other authors:
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Universitat de Barcelona |
Abstract:
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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. |
Subject(s):
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-Bicapes lipídiques -Proteïnes quinases -Transducció de senyal cel·lular -Membranes cel·lulars -Lipid bilayers -Protein kinases -Cellular signal transduction -Cell membranes |
Rights:
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cc by-nc (c) Le Roux et al., 2016
http://creativecommons.org/licenses/by-nd/3.0/es/ |
Document type:
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Article Article - Published version |
Published by:
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Wiley-VCH
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