期刊
CELL HOST & MICROBE
卷 9, 期 2, 页码 125-136出版社
CELL PRESS
DOI: 10.1016/j.chom.2011.01.009
关键词
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资金
- NSF [IOS-0929410, MCB-0718882]
- DOE [DE-FG05-95ER20187]
- Ohio Agricultural Research and Development Center of The Ohio State University
- The Ohio State University
- NIH
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [0929410] Funding Source: National Science Foundation
The Arabidopsis NB-LRR immune receptor RPM1 recognizes the Pseudomonas syringae type III effectors AvrB or AvrRpm1 to mount an immune response. Although neither effector is itself a kinase, AvrRpm1 and AvrB are known to target Arabidopsis RIN4, a negative regulator of basal plant defense, for phosphorylation. We show that RIN4 phosphorylation activates RPM1. RIN4(142-176) is necessary and, with appropriate localization sequences, sufficient to support effector-triggered RPM1 activation, with the threonine residue at position 166 being critical. Phosphomimic substitutions at T166 cause effector-independent RPM1 activation. RIN4 T166 is phosphorylated in vivo in the presence of AvrB or AvrRpm1. RIN4 mutants that lose interaction with AvrB cannot be coimmunoprecipitated with RPM1. This defines a common interaction platform required for RPM1 activation by phosphorylated RIN4 in response to pathogenic effectors. Conservation of an analogous threonine across all RIN4-like proteins suggests a key function for this residue beyond the regulation of RPM1.
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