CLE peptides in plants: proteolytic processing, structure-activity relationship, and ligand-receptor interaction

J Integr Plant Biol. 2012 Oct;54(10):738-45. doi: 10.1111/j.1744-7909.2012.01154.x.

Abstract

Ligand-receptor signaling initiated by the CLAVATA3/ ENDOSPERM SURROUNDING REGION (CLE) family peptides is critical in regulating cell division and differentiation in meristematic tissues in plants. Biologically active CLE peptides are released from precursor proteins via proteolytic processing. The mature form of CLE ligands consists of 12-13 amino acids with several post-translational modifications. This review summarizes recent progress toward understanding the proteolytic activities that cleave precursor proteins to release CLE peptides, the molecular structure and function of mature CLE ligands, and interactions between CLE ligands and corresponding leucine-rich repeat (LRR) receptor-like kinases (RLKs).

Publication types

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

MeSH terms

  • Arabidopsis / cytology
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Cell Differentiation / genetics
  • Cell Differentiation / physiology
  • Cell Division / genetics
  • Cell Division / physiology
  • Meristem / cytology
  • Meristem / metabolism
  • Protein Binding
  • Structure-Activity Relationship

Substances

  • AT2G27250 protein, Arabidopsis
  • Arabidopsis Proteins