Plant intracellular innate immune receptor Resistance to Pseudomonas syringae pv. maculicola 1 (RPM1) is activated at, and functions on, the plasma membrane

Zhiyong Gao, Eui Hwan Chung, Timothy K. Eitas, Jeffery L. Dangl

Research output: Contribution to journalArticlepeer-review

119 Citations (Scopus)

Abstract

Plants deploy intracellular innate immune receptors to recognize pathogens and initiate disease resistance. These nucleotide-binding, leucine-rich repeat (NB-LRR) proteins are activated by pathogen effector proteins that are delivered into the host cell to suppress host defense responses. Little is known about the sites and mechanisms of NB-LRR activation, but some NB-LRR proteins can function inside the plant nucleus. We demonstrate that RPM1 is activated on the plasma membrane and does not relocalize to the nucleus. An autoactive RPM1(D505V) allele that recapitulates key features of normal RPM1 activation also resides on the plasmamembrane. There is no detectable relocalization of activated RPM1 to the nucleus. Hindering potential nuclear entry of RPM1-Myc did not affect either its effector-triggered hypersensitive-response (HR) cell death or its disease resistance functions, further suggesting that nuclear translocation is not required for RPM1 function. RPM1 tethered onto the plasma membrane with a dual acylated N-terminal epitope tag retained the ability to mediate HR, consistent with this RPM1 function being activated on the plasma membrane. Plant NBLRR proteins can thus function at various locations in the cell.

Original languageEnglish
Pages (from-to)7619-7624
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume108
Issue number18
DOIs
Publication statusPublished - 2011 May 3
Externally publishedYes

Keywords

  • Plant disease resistance
  • Plant nucleotide-binding leucine-rich repeat receptor immune receptor
  • Type III bacterial effectors

ASJC Scopus subject areas

  • General

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