title: CLE peptides in plants: proteolytic processing, structure-activity relationship, and ligand-receptor interaction.
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).
authors.affiliation: Tobacco Research Institute, Chinese Academy of Agricultural Sciences/Key Laboratory of Tobacco Biology and Processing, Ministry of Agriculture, Qingdao 266101, China.
authors.forename: Xiaoming
authors.initials: X
authors.lastname: Gao
authors.forename: Yongfeng
authors.initials: Y
authors.lastname: Guo
mesh_terms: D017360:Arabidopsis / Q000166:cytology / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D002454:Cell Differentiation / Q000235:genetics / Q000502:physiology; D002455:Cell Division / Q000235:genetics / Q000502:physiology; D018519:Meristem / Q000166:cytology / Q000378:metabolism; D011485:Protein Binding; D013329:Structure-Activity Relationship
chemical_list: C118167:AT2G27250 protein, Arabidopsis; D029681:Arabidopsis Proteins