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

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 alway...

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Autores: Le Roux, Anabel-Lise, Castro, Bruno, Garbacik, Erik T., García-Parajó, Maria F., Pons Vallès, Miquel
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2016
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/97403
Acceso en línea:https://hdl.handle.net/2445/97403
Access Level:acceso abierto
Palabra clave:Bicapes lipídiques
Proteïnes quinases
Transducció de senyal cel·lular
Membranes cel·lulars
Lipid bilayers
Protein kinases
Cellular signal transduction
Cell membranes
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spelling Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayersLe Roux, Anabel-LiseCastro, BrunoGarbacik, Erik T.García-Parajó, Maria F.Pons Vallès, MiquelBicapes lipídiquesProteïnes quinasesTransducció de senyal cel·lularMembranes cel·lularsLipid bilayersProtein kinasesCellular signal transductionCell membranesThe 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.Wiley-VCH2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/97403Articles publicats en revistes (Química Inorgànica i Orgànica)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: http://dx.doi.org/10.1002/slct.201600117ChemistrySelect, 2016, vol. 1, num. 4, p. 642-647http://dx.doi.org/10.1002/slct.201600117cc by-nc (c) Le Roux et al., 2016http://creativecommons.org/licenses/by-nd/3.0/es/info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/974032026-05-27T06:46:51Z
dc.title.none.fl_str_mv Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
title Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
spellingShingle Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
Le Roux, Anabel-Lise
Bicapes lipídiques
Proteïnes quinases
Transducció de senyal cel·lular
Membranes cel·lulars
Lipid bilayers
Protein kinases
Cellular signal transduction
Cell membranes
title_short Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
title_full Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
title_fullStr Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
title_full_unstemmed Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
title_sort Single molecule fluorescence reveals dimerization of myristoylated Src N-terminal region on supported lipid bilayers
dc.creator.none.fl_str_mv Le Roux, Anabel-Lise
Castro, Bruno
Garbacik, Erik T.
García-Parajó, Maria F.
Pons Vallès, Miquel
author Le Roux, Anabel-Lise
author_facet Le Roux, Anabel-Lise
Castro, Bruno
Garbacik, Erik T.
García-Parajó, Maria F.
Pons Vallès, Miquel
author_role author
author2 Castro, Bruno
Garbacik, Erik T.
García-Parajó, Maria F.
Pons Vallès, Miquel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Bicapes lipídiques
Proteïnes quinases
Transducció de senyal cel·lular
Membranes cel·lulars
Lipid bilayers
Protein kinases
Cellular signal transduction
Cell membranes
topic Bicapes lipídiques
Proteïnes quinases
Transducció de senyal cel·lular
Membranes cel·lulars
Lipid bilayers
Protein kinases
Cellular signal transduction
Cell membranes
description 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.
publishDate 2016
dc.date.none.fl_str_mv 2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/97403
url https://hdl.handle.net/2445/97403
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: http://dx.doi.org/10.1002/slct.201600117
ChemistrySelect, 2016, vol. 1, num. 4, p. 642-647
http://dx.doi.org/10.1002/slct.201600117
dc.rights.none.fl_str_mv cc by-nc (c) Le Roux et al., 2016
http://creativecommons.org/licenses/by-nd/3.0/es/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc by-nc (c) Le Roux et al., 2016
http://creativecommons.org/licenses/by-nd/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley-VCH
publisher.none.fl_str_mv Wiley-VCH
dc.source.none.fl_str_mv Articles publicats en revistes (Química Inorgànica i Orgànica)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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