Premium
CLE Peptides in Plants: Proteolytic Processing, Structure‐Activity Relationship, and Ligand‐Receptor Interaction F
Author(s) -
Gao Xiaoming,
Guo Yongfeng
Publication year - 2012
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/j.1744-7909.2012.01154.x
Subject(s) - ligand (biochemistry) , biochemistry , receptor , meristem , proteolytic enzymes , amino acid , biology , function (biology) , endosperm , microbiology and biotechnology , aminopeptidase , chemistry , leucine , enzyme , gene
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).[ Yongfeng Guo (Corresponding author)]