Nucleocytoplasmic partitioning of tobacco N receptor is modulated by SGT1

© 2013 The Authors. New Phytologist © 2013 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 200(2013), 1 vom: 19. Okt., Seite 158-171
1. Verfasser: Hoser, Rafał (VerfasserIn)
Weitere Verfasser: Żurczak, Marek, Lichocka, Małgorzata, Zuzga, Sabina, Dadlez, Michal, Samuel, Marcus A, Ellis, Brian E, Stuttmann, Johannes, Parker, Jane E, Hennig, Jacek, Krzymowska, Magdalena
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... Mitogen-Activated Protein Kinases EC 2.7.11.24 SA-induced protein kinase
Beschreibung
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