Plant NB-LRR signaling: upstreams and downstreams

Curr Opin Plant Biol. 2011 Aug;14(4):365-71. doi: 10.1016/j.pbi.2011.03.011. Epub 2011 Mar 31.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Cell Nucleus / genetics
  • Cell Nucleus / metabolism
  • Cytoplasm / genetics
  • Cytoplasm / metabolism
  • Disease Resistance*
  • Gene Expression Regulation, Plant
  • HSP90 Heat-Shock Proteins / metabolism*
  • Host-Pathogen Interactions
  • Phosphorylation
  • Plant Proteins / metabolism
  • Plants / genetics
  • Plants / immunology*
  • Plants / metabolism
  • Protein Stability
  • Proteins / immunology*
  • Proteins / metabolism
  • Signal Transduction*

Substances

  • HSP90 Heat-Shock Proteins
  • Plant Proteins
  • Proteins
  • leucine-rich repeat proteins