Leucine-rich repeat receptor kinases in plants: structure, function, and signal transduction pathways

Int Rev Cytol. 2004;234:1-46. doi: 10.1016/S0074-7696(04)34001-5.

Abstract

Leucine-rich repeat receptor kinases (LRR-RKs) comprise the largest subfamily of transmembrane receptor-like kinases in plants, with over 200 members in Arabidopsis. LRR-RKs regulate a wide variety of developmental and defense-related processes including cell proliferation, stem cell maintenance, hormone perception, host-specific as well as non-host-specific defense response, wounding response, and symbiosis. Several studies indicate that LRR-RKs act as dimers, and some may form a receptor complex with leucine-rich repeat receptor-like proteins (LRR-RPs) that lack a cytoplasmic kinase domain. Despite the fact that structural features of LRR-RKs are fairy similar, five available ligand molecules for LRR-RKs are structurally diverse, from steroids (brassinolides) to peptides (phytosulfokine and systemin) and secreted proteins (CLV3). Precise ligand-binding sites of LRR-RKs are not understood. However, the extracellular "island" domain that intercepts the LRR domain in some LRR-RKs may play an important role in ligand binding. Advances in unveiling components of three LRR-RK signaling pathways, namely BRI1 in steroid signaling, CLV1 in meristem maintenance, and FLS2 in bacterial elicitor perception, revealed an intriguing link between plant LRR-RK and animal receptor signaling pathways. Finally, rapid progress made in LRR-RK research beyond the model system Arabidopsis has provided exciting, novel insights into the evolution of the LRR-RK signaling system in plants, such as BRI1 utilized in the wound-responsive signaling pathway in Solanaceae plants and recruitment of CLV1 in nodule development in leguminous plants.

Publication types

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

MeSH terms

  • Binding Sites / physiology
  • Ligands
  • Plant Development*
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Plants / enzymology*
  • Plants / genetics
  • Protein Kinases / genetics
  • Protein Kinases / metabolism*
  • Protein Structure, Tertiary / physiology
  • Signal Transduction / physiology*

Substances

  • Ligands
  • Plant Proteins
  • Protein Kinases