The polyproline-motif of S6K2: eIF5A translational dependence and importance for protein-protein interactions

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dc.contributorLETA - Laboratório de Toxinologia Aplicadapt_BR
dc.contributorCentro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributor.authorMeneguello, Leticiapt_BR
dc.contributor.authorBarbosa, Natália M.pt_BR
dc.contributor.authorPereira, Karina D.pt_BR
dc.contributor.authorProença, André R. G.pt_BR
dc.contributor.authorTamborlin, Leticiapt_BR
dc.contributor.authorSimabuco, Fernando M.pt_BR
dc.contributor.authorIwai, Leo Keipt_BR
dc.contributor.authorZanelli, Cleslei F.pt_BR
dc.contributor.authorValentini, Sandro R.pt_BR
dc.contributor.authorLuchessi, Augusto D.pt_BR
dc.date.accessioned2020-07-09T21:23:04Z-
dc.date.available2020-07-09T21:23:04Z-
dc.date.issued2019pt_BR
dc.identifier.citationMeneguello L, Barbosa NM., Pereira KD., Proença AR.G., Tamborlin L, Simabuco FM., et al. The polyproline-motif of S6K2: eIF5A translational dependence and importance for protein-protein interactions. J Cell Biochem. 2019 Apr;120(4):6015-6025. doi:10.1002/jcb.27888.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2682-
dc.description.abstractRibosomal S6 kinase 1 (S6K1) and S6K2 proteins are effectors of the mammalian target of rapamycin complex 1 pathway, which control the process of protein synthesis in eukaryotes. S6K2 is associated with tumor progression and has a conserved C-terminus polyproline rich motif predicted to be important for S6K2 interactions. It is noteworthy that the translation of proteins containing sequential prolines has been proposed to be dependent of eukaryotic translation initiation factor 5A (eIF5A) translation factor. Therefore, we investigated the importance of polyproline-rich region of the S6K2 for its intrinsic phosphorylation activity, protein-protein interaction and eIF5A role in S6K2 translation. In HeLa cell line, replacing S6K2 polyproline by the homologous S6K1-sequence did not affect its kinase activity and the S6K2 endogenous content was maintained after eIF5A gene silencing, even after near complete depletion of eIF5A protein. Moreover, no changes in S6K2 transcript content was observed, ruling out the possibility of compensatory regulation by increasing the mRNA content. However, in the budding yeast model, we observed that S6K2 production was impaired when compared with S6K2?Pro, after reduction of eIF5A protein content. These results suggest that although the polyproline region of S6K2 is capable of generating ribosomal stalling, the depletion of eIF5A in HeLa cells seems to be insufficient to cause an expressive decrease in the content of endogenous S6K2. Finally, coimmunoprecipitation assays revealed that the replacement of the polyproline motif of S6K2 alters its interactome and impairs its interaction with RPS6, a key modulator of ribosome activity. These results evidence the importance of S6K2 polyproline motif in the context of S6Ks function.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.format.extentp. 6015-6025pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofJournal of Cellular Biochemistrypt_BR
dc.titleThe polyproline-motif of S6K2: eIF5A translational dependence and importance for protein-protein interactionspt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1002/jcb.27888pt_BR
dc.identifier.urlhttp://dx.doi.org/10.1002/jcb.27888pt_BR
dc.contributor.externalUniversidade Estadual de Campinas (UNICAMP)¦¦Brasilpt_BR
dc.contributor.externalUniversidade Estadual Paulista Júlio de Mesquita Filho (UNESP)¦¦Brasilpt_BR
dc.identifier.citationvolume120pt_BR
dc.identifier.citationissue4pt_BR
dc.subject.keywordeukaryotic translation initiation factor 5Apt_BR
dc.subject.keywordpolyprolinept_BR
dc.subject.keywordprotein interactionpt_BR
dc.subject.keywordribosomal protein L7apt_BR
dc.subject.keywordribosomal protein S6pt_BR
dc.subject.keywordribosomal S6 kinase 2pt_BR
dc.subject.keywordribosomal protein S6 kinasespt_BR
dc.relation.ispartofabbreviatedJ Cell Biochempt_BR
dc.identifier.citationabntv. 120, n. 4, p. 6015-6025, abr. 2019pt_BR
dc.identifier.citationvancouver2019 Apr;120(4):6015-6025pt_BR
dc.contributor.butantanIwai, Leo Kei|:Pesquisador:Docente Colaborador PPGTOX|:Laboratório Especial de Toxinologia Aplicada (LETA)|:pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/07467-1pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2010/18095-0pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2012/13558-7pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.openairetypeArticle-
item.fulltextCom Texto completo-
item.grantfulltextembargo_29990101-
item.languageiso639-1English-
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