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Conserved threonine residues within the A-loop of the receptor NIK differentially regulate the kinase function required for antiviral signaling.

التفاصيل البيبلوغرافية
العنوان: Conserved threonine residues within the A-loop of the receptor NIK differentially regulate the kinase function required for antiviral signaling.
المؤلفون: Anésia A Santos, Claudine M Carvalho, Lilian H Florentino, Humberto J O Ramos, Elizabeth P B Fontes
المصدر: PLoS ONE, Vol 4, Iss 6, p e5781 (2009)
بيانات النشر: Public Library of Science (PLoS), 2009.
سنة النشر: 2009
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: 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.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
Relation: https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19492062/pdf/?tool=EBI; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0005781
URL الوصول: https://doaj.org/article/8552e281e3204422b46c151129a59e58
رقم الأكسشن: edsdoj.8552e281e3204422b46c151129a59e58
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0005781