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Campo DC | Valor | Idioma |
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dc.contributor.author | Santos, Anésia A. | |
dc.contributor.author | Carvalho, Claudine M. | |
dc.contributor.author | Florentino, Lilian H. | |
dc.contributor.author | Ramos, Humberto J. O. | |
dc.contributor.author | Fontes, Elizabeth P. B. | |
dc.date.accessioned | 2017-11-01T10:19:45Z | |
dc.date.available | 2017-11-01T10:19:45Z | |
dc.date.issued | 2009-06-03 | |
dc.identifier.issn | 1932-6203 | |
dc.identifier.uri | http://dx.doi.org/10.1371/journal.pone.0005781 | |
dc.identifier.uri | http://www.locus.ufv.br/handle/123456789/12670 | |
dc.description.abstract | NSP-interacting kinase (NIK1) is a receptor-like kinase identified as a virulence target of the begomovirus nuclear shuttle protein (NSP). We found that NIK1 undergoes a stepwise pattern of phosphorylation within its activation-loop domain (A- loop) with distinct roles for different threonine residues. Mutations at Thr-474 or Thr-468 impaired autophosphorylation and were defective for kinase activation. In contrast, a mutation at Thr-469 did not impact autophosphorylation and increased substrate phosphorylation, suggesting an inhibitory role for Thr-469 in kinase function. To dissect the functional significance of these results, we used NSP-expressing virus infection as a mechanism to interfere with wild type and mutant NIK1 action in plants. The NIK1 knockout mutant shows enhanced susceptibility to virus infections, a phenotype that could be complemented with ectopic expression of a 35S-NIK1 or 35S-T469A NIK1 transgenes. However, ectopic expression of an inactive kinase or the 35S-T474A NIK1 mutant did not reverse the enhanced susceptibility phenotype of knockout lines, demonstrating that Thr-474 autophosphorylation was needed to transduce a defense response to geminiviruses. Furthermore, mutations at Thr-474 and Thr-469 residues antagonistically affected NIK-mediated nuclear relocation of the downstream effector rpL10. These results establish that NIK1 functions as an authentic defense receptor as it requires activation to elicit a defense response. Our data also suggest a model whereby phosphorylation-dependent activation of a plant receptor-like kinase enables the A-loop to control differentially auto- and substrate phosphorylation. | en |
dc.format | pt-BR | |
dc.language.iso | eng | pt-BR |
dc.publisher | Plos One | pt-BR |
dc.relation.ispartofseries | 4(6): e5781, June 2009 | pt-BR |
dc.rights | Open Access | pt-BR |
dc.subject | Receptor NIK | pt-BR |
dc.subject | Antiviral signaling | pt-BR |
dc.title | Conserved threonine residues within the A-Loop of the receptor NIK differentially regulate the kinase function required for antiviral signaling | en |
dc.type | Artigo | pt-BR |
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