Article

Plant NB-LRR signaling: upstreams and downstreams.

Department of Plant Pathology, University of California, Davis, CA 95616, United States.
Current opinion in plant biology (impact factor: 10.33). 03/2011; 14(4):365-71. DOI:10.1016/j.pbi.2011.03.011 pp.365-71
Source: PubMed

ABSTRACT Plant disease resistance proteins commonly belong to the nucleotide binding-leucine rich repeat (NB-LRR) protein family. These specialized immune proteins mediate recognition of diverse pathogen-derived effector proteins and initiate potent defense responses. NB-LRRs exhibit a multidomain architecture and each domain appears to have discrete functions depending on the stage of NB-LRR signaling. Novel proteins that were found to interact with the core HSP90 chaperone complex regulate accumulation and activation of NB-LRR immune receptors. Recent studies have also advanced our understanding of how accessory proteins contribute to NB-LRR activation. The dynamic nature of NB-LRR localization to different subcellular compartments before and after activation suggests that NB-LRRs may activate immune responses in multiple parts of the cell. In this review we highlight recent advances in understanding NB-LRR function.

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    Article: Nuclear accumulation of the Arabidopsis immune receptor RPS4 is necessary for triggering EDS1-dependent defense.
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Keywords

accessory proteins
 
accumulation
 
core HSP90 chaperone complex
 
different subcellular compartments
 
diverse pathogen-derived effector proteins
 
dynamic nature
 
multidomain architecture
 
multiple parts
 
NB-LRR immune receptors
 
NB-LRRs
 
Novel proteins
 
nucleotide binding-leucine rich repeat
 
Plant disease resistance proteins
 
potent defense responses
 
recent advances
 
Recent studies
 
specialized immune proteins
 
understanding NB-LRR function
 

James Mitch Elmore