Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers

التفاصيل البيبلوغرافية
العنوان: Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
المؤلفون: Maria F. Garcia Parajo, Anabel-Lise Le Roux, E.T. Garbacik, Miquel Pons, Bruno Castro
المساهمون: Universitat de Barcelona
المصدر: Dipòsit Digital de la UB
Universidad de Barcelona
Recercat. Dipósit de la Recerca de Catalunya
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بيانات النشر: Wiley-VCH, 2016.
سنة النشر: 2016
مصطلحات موضوعية: 0301 basic medicine, Cell signaling, Cellular signal transduction, Lipid bilayers, Biology, 010402 general chemistry, 01 natural sciences, SH3 domain, Green fluorescent protein, 03 medical and health sciences, Protein kinases, Protein myristoylation, Lipid bilayer, Myristoylation, Tyrosine-protein kinase CSK, Bicapes lipídiques, Transducció de senyal cel·lular, General Chemistry, 0104 chemical sciences, Proteïnes quinases, Cell membranes, 030104 developmental biology, Biochemistry, Biophysics, Membranes cel·lulars, Proto-oncogene tyrosine-protein kinase Src
الوصف: 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.
وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a459093cc2b6738cc8ae970274548b5cTest
http://hdl.handle.net/2445/97403Test
حقوق: OPEN
رقم الانضمام: edsair.doi.dedup.....a459093cc2b6738cc8ae970274548b5c
قاعدة البيانات: OpenAIRE