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dc.contributor.authorOliva-Martinez, Jose Luis 
dc.contributor.authorZarich-Dimitrievich, Natasha 
dc.contributor.authorMartinez, Natalia 
dc.contributor.authorJorge, Rocío
dc.contributor.authorCastrillo, Antonio
dc.contributor.authorAzañedo, Marta
dc.contributor.authorGarcia-Vargas , Susana 
dc.contributor.authorGutiérrez-Eisman, Silvia
dc.contributor.authorJuarranz, Angeles
dc.contributor.authorBoscá, Lisardo
dc.contributor.authorGutkind, J Silvio
dc.contributor.authorRojas-Cabañeros, Jose Maria 
dc.date.accessioned2020-04-23T07:00:48Z
dc.date.available2020-04-23T07:00:48Z
dc.date.issued2004-08-06
dc.identifier.citationJ Biol Chem. 2004 Aug 6;279(32):33480-91. Epub 2004 Jun 4.es_ES
dc.identifier.issn0021-9258es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/9698
dc.descriptionRetraction in: The P34G mutation reduces the transforming activity of K-Ras and N-Ras in NIH 3T3 cells but not of H-Ras. [J Biol Chem. 2018]es_ES
dc.description.abstractRas proteins (H-, N-, and K-Ras) operate as molecular switches in signal transduction cascades controlling cell proliferation, differentiation, or apoptosis. The interaction of Ras with its effectors is mediated by the effector-binding loop, but different data about Ras location to plasma membrane subdomains and new roles for some docking/scaffold proteins point to signaling specificities of the different Ras proteins. To investigate the molecular mechanisms for these specificities, we compared an effector loop mutation (P34G) of three Ras isoforms (H-, N-, and K-Ras4B) for their biological and biochemical properties. Although this mutation diminished the capacity of Ras proteins to activate the Raf/ERK and the phosphatidylinositol 3-kinase/AKT pathways, the H-Ras V12G34 mutant retained the ability to cause morphological transformation of NIH 3T3 fibroblasts, whereas both the N-Ras V12G34 and the K-Ras4B V12G34 mutants were defective in this biological activity. On the other hand, although both the N-Ras V12G34 and the K-Ras4B V12G34 mutants failed to promote activation of the Ral-GDS/Ral A/PLD and the Ras/Rac pathways, the H-Ras V12G34 mutant retained the ability to activate these signaling pathways. Interestingly, the P34G mutation reduced specifically the N-Ras and K-Ras4B in vitro binding affinity to Ral-GDS, but not in the case of H-Ras. Thus, independently of Ras location to membrane subdomains, there are marked differences among Ras proteins in the sensitivity to an identical mutation (P34G) affecting the highly conserved effector-binding loop.es_ES
dc.description.sponsorshipThis work was supported in part by Programa General del Conocimiento (BMC2001-0057), Intramural Instituto de Salud Carlos III (ISCIII) (01/16), and SAF2003-02604 (Ministerio de Ciencia y Tecnología) grants (to J. M. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biology (ASBMB) es_ES
dc.type.hasVersionVoRes_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAnimals es_ES
dc.subject.meshBinding Sites es_ES
dc.subject.meshDNA-Binding Proteins es_ES
dc.subject.meshEnzyme Activation es_ES
dc.subject.meshGene Expression es_ES
dc.subject.meshGenes, ras es_ES
dc.subject.meshHumans es_ES
dc.subject.meshMice es_ES
dc.subject.meshMitogen-Activated Protein Kinase 1 es_ES
dc.subject.meshMitogen-Activated Protein Kinase 3 es_ES
dc.subject.meshMitogen-Activated Protein Kinases es_ES
dc.subject.meshNIH 3T3 Cells es_ES
dc.subject.meshPhosphatidylinositol 3-Kinases es_ES
dc.subject.meshPhospholipase D es_ES
dc.subject.meshProtein Isoforms es_ES
dc.subject.meshProtein-Serine-Threonine Kinases es_ES
dc.subject.meshProto-Oncogene Proteins es_ES
dc.subject.meshProto-Oncogene Proteins c-akt es_ES
dc.subject.meshProto-Oncogene Proteins c-raf es_ES
dc.subject.meshSignal Transduction es_ES
dc.subject.meshStructure-Activity Relationship es_ES
dc.subject.meshTranscription Factors es_ES
dc.subject.meshTransfection es_ES
dc.subject.meshets-Domain Protein Elk-1 es_ES
dc.subject.meshrac1 GTP-Binding Protein es_ES
dc.subject.meshral GTP-Binding Proteins es_ES
dc.subject.meshral Guanine Nucleotide Exchange Factor es_ES
dc.subject.meshras Proteins es_ES
dc.subject.meshMutation es_ES
dc.titleThe P34G mutation reduces the transforming activity of K-Ras and N-Ras in NIH 3T3 cells but not of H-Rases_ES
dc.typejournal articlees_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.identifier.pubmedID15181015es_ES
dc.format.volume279es_ES
dc.format.number32es_ES
dc.format.page33480-91es_ES
dc.identifier.doi10.1074/jbc.M404058200es_ES
dc.contributor.funderInstituto de Salud Carlos III 
dc.contributor.funderMinisterio de Ciencia y Tecnología (España) 
dc.description.peerreviewedes_ES
dc.relation.publisherversionhttps://doi.org/10.1074/jbc.M404058200es_ES
dc.identifier.journalThe Journal of biological chemistryes_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu_repo/grantAgreement/ES/BMC2001-0057es_ES
dc.relation.projectIDinfo:eu_repo/grantAgreement/ES/SAF2003-02604es_ES
dc.rights.accessRightsopen accesses_ES


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