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
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520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a MAPK 
650 4 |a NB-LRR 
650 4 |a SGT1 
650 4 |a disease resistance 
650 4 |a nucleocytoplasmic shuttling 
650 4 |a protein phosphorylation 
650 4 |a tobacco (Nicotiana tabacum) 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Mitogen-Activated Protein Kinases  |2 NLM 
650 7 |a EC 2.7.11.24  |2 NLM 
650 7 |a SA-induced protein kinase  |2 NLM 
650 7 |a EC 2.7.11.24  |2 NLM 
700 1 |a Żurczak, Marek  |e verfasserin  |4 aut 
700 1 |a Lichocka, Małgorzata  |e verfasserin  |4 aut 
700 1 |a Zuzga, Sabina  |e verfasserin  |4 aut 
700 1 |a Dadlez, Michal  |e verfasserin  |4 aut 
700 1 |a Samuel, Marcus A  |e verfasserin  |4 aut 
700 1 |a Ellis, Brian E  |e verfasserin  |4 aut 
700 1 |a Stuttmann, Johannes  |e verfasserin  |4 aut 
700 1 |a Parker, Jane E  |e verfasserin  |4 aut 
700 1 |a Hennig, Jacek  |e verfasserin  |4 aut 
700 1 |a Krzymowska, Magdalena  |e verfasserin  |4 aut 
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773 1 8 |g volume:200  |g year:2013  |g number:1  |g day:19  |g month:10  |g pages:158-171 
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