Abstract

Plants are exposed to numerous potential pathogenic microbes. To counter the threat, plants have evolved diverse pattern- recognition receptors (PRRs), which are receptor kinases (RKs) and receptor proteins (RPs) specialized to detect conserved pathogen/microbe-associated molecular patterns (PAMPs/MAMPs). Although only a handful of RKs and RPs are known PRRs, they belong to the receptor-like kinase (RLK) and receptor-like protein (RLP) superfamilies that undergo lineage-specific expansion, suggesting that many of these RLKs and RLPs are potential PRRs. Analyses of existing PRRs have uncovered ligand-induced RLK-RK or RLK-RP oligomerization as a common mechanism for immune activation. PRRs can recruit additional components to form dynamic receptor complexes, which mediate specific cellular responses. Detailed analyses of these components are shedding light on molecular mechanisms underlying the regulation of PRR activity and downstream signaling.

Highlights

  • Unlike animals, plants lack an adaptive immune system, and entirely rely on innate immunity to resist numerous potential pathogens in their environment (Jones and Dangl, 2006; Boller and Felix, 2009)

  • pathogen-associated molecular patterns (PAMPs) can be detected by surface-localized pattern-recognition receptors (PRRs) that are receptor kinases (RKs) or receptor proteins (RPs), thereby activating pattern-triggered immunity (PTI)

  • Increasing evidences support that the receptor-like kinases (RLKs) and receptor-like proteins (RLPs) super families play a crucial role in the perception of diverse microbial and endogenous patterns, forming a powerful surveillance system at the cell surface against invading microbes and insects

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Summary

Life Sciences

State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China Received May 20, 2016; accepted June 2, 2016; published online August 16, 2016

INTRODUCTION
RLKS AND RLPS BELONG TO SUPER FAMILIES IN HIGHER PLANTS
RKS AND RPS AS PRRS
OLIGOMERIZATION AS A COMMON MECHANISM FOR PRR ACTIVATION
RLCKS LINK PRRS WITH DOWNSTREAM SIGNALING
DYNAMIC REGULATION OF PRR COMPLEXES
CONCLUDING REMARKS
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