]*>","")" /> CLE Peptides in Plants: Proteolytic Processing, Structure-Activity Relationship, and Ligand-Receptor Interaction

J Integr Plant Biol ›› 2012, Vol. 54 ›› Issue (10): 738-745.DOI: 10.1111/j.1744-7909.2012.01154.x

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CLE Peptides in Plants: Proteolytic Processing, Structure-Activity Relationship, and Ligand-Receptor Interaction

Xiaoming Gao and Yongfeng Guo*   

  • 收稿日期:2012-07-31 接受日期:2012-08-19 出版日期:2012-10-01 发布日期:2012-08-24

CLE Peptides in Plants: Proteolytic Processing, Structure-Activity Relationship, and Ligand-Receptor Interaction

Xiaoming Gao and Yongfeng Guo*   

  1. Tobacco Research Institute, Chinese Academy of Agricultural Sciences / Key Laboratory of Tobacco Biology and Processing, Ministry of Agriculture, Qingdao 266101, China
  • Received:2012-07-31 Accepted:2012-08-19 Online:2012-10-01 Published:2012-08-24
  • About author:*Corresponding author Tel: +86 532 6671 5256; Fax: +86 532 8870 2056; E-mail: yongfeng.guo@gmail.com

被引次数

40

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).

Gao X, Guo Y (2012) CLE peptides in plants: Proteolytic processing, structure-activity relationship, and ligand-receptor interaction. J. Integr. Plant Biol. 54(10), 738–745.

Key words: CLV3, leucine-rich repeat receptor-like kinase, meristem, nodulation, stem cell

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