Abstract
Plant disease resistance can be triggered by specific recognition of microbial effectors by plant nucleotide binding-leucine rich repeat (NB-LRR) receptors. Over the last few years, many efforts have greatly improved the understanding of effector and NB-LRR function, but have left a lot of questions as to how effector perception activates NB-LRR induction of defense signaling. This review describes exciting new findings showing similarities and differences in function of diverse plant NB-LRR proteins in terms of pathogen recognition and where and how resistance proteins are activated. Localization studies have shown that some NB-LRRs can activate signaling from the cytosol while others act in the nucleus. Also, the structural determination of two NB-LRR signaling domains demonstrated that receptor oligomerization is fundamental for the activation of resistance signaling.
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