Nucleocytoplasmic partitioning of tobacco N receptor is modulated by SGT1
© 2013 The Authors. New Phytologist © 2013 New Phytologist Trust.
Veröffentlicht in: | The New phytologist. - 1979. - 200(2013), 1 vom: 19. Okt., Seite 158-171 |
---|---|
1. Verfasser: | |
Weitere Verfasser: | , , , , , , , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2013
|
Zugriff auf das übergeordnete Werk: | The New phytologist |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't MAPK NB-LRR SGT1 disease resistance nucleocytoplasmic shuttling protein phosphorylation tobacco (Nicotiana tabacum) Plant Proteins mehr... |
Zusammenfassung: | © 2013 The Authors. New Phytologist © 2013 New Phytologist Trust. SGT1 (Suppressor of G2 allele of SKP1) is required to maintain plant disease Resistance (R) proteins with Nucleotide-Binding (NB) and Leucine-Rich Repeat (LRR) domains in an inactive but signaling-competent state. SGT1 is an integral component of a multi-protein network that includes RACK1, Rac1, RAR1, Rboh, HSP90 and HSP70, and in rice the Mitogen-Activated Protein Kinase (MAPK), OsMAPK6. Tobacco (Nicotiana tabacum) N protein, which belongs to the Toll-Interleukin Receptor (TIR)-NB-LRR class of R proteins, confers resistance to Tobacco Mosaic Virus (TMV). Following transient expression in planta, we analyzed the functional relationship between SGT1, SIPK - a tobacco MAPK6 ortholog - and N, using mass spectrometry, confocal microscopy and pathogen assays. Here, we show that tobacco SGT1 undergoes specific phosphorylation in a canonical MAPK target-motif by SIPK. Mutation of this motif to mimic SIPK phosphorylation leads to an increased proportion of cells displaying SGT1 nuclear accumulation and impairs N-mediated resistance to TMV, as does phospho-null substitution at the same residue. Forced nuclear localization of SGT1 causes N to be confined to nuclei. Our data suggest that one mode of regulating nucleocytoplasmic partitioning of R proteins is by maintaining appropriate levels of SGT1 phosphorylation catalyzed by plant MAPK |
---|---|
Beschreibung: | Date Completed 15.04.2014 Date Revised 13.12.2023 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1469-8137 |
DOI: | 10.1111/nph.12347 |