Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 125-136 |
| Number of pages | 12 |
| Journal | Cell Host and Microbe |
| Volume | 9 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 17 2011 |
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ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Cancer Research
- Molecular Biology
Cite this
Specific threonine phosphorylation of a host target by two unrelated type III effectors activates a host innate immune receptor in plants. / Chung, Eui Hwan; Da Cunha, Luis; Wu, Ai Jiuan; Gao, Zhiyong; Cherkis, Karen; Afzal, Ahmed; MacKey, David; Dangl, Jeffery L.
In: Cell Host and Microbe, Vol. 9, No. 2, 17.02.2011, p. 125-136.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Specific threonine phosphorylation of a host target by two unrelated type III effectors activates a host innate immune receptor in plants
AU - Chung, Eui Hwan
AU - Da Cunha, Luis
AU - Wu, Ai Jiuan
AU - Gao, Zhiyong
AU - Cherkis, Karen
AU - Afzal, Ahmed
AU - MacKey, David
AU - Dangl, Jeffery L.
PY - 2011/2/17
Y1 - 2011/2/17
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=79951639951&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79951639951&partnerID=8YFLogxK
U2 - 10.1016/j.chom.2011.01.009
DO - 10.1016/j.chom.2011.01.009
M3 - Article
C2 - 21320695
AN - SCOPUS:79951639951
VL - 9
SP - 125
EP - 136
JO - Cell Host and Microbe
JF - Cell Host and Microbe
SN - 1931-3128
IS - 2
ER -