Calreticulin: conserved protein and diverse functions in plants

• Published in: Physiologia plantarum Vol. 136; no. 2; pp. 127 - 138
• Main Authors: Jia, Xiao-Yun, He, Li-Heng, Jing, Rui-Lian, Li, Run-Zhi
• Format: Journal Article
• Language: English
• Published: Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.06.2009; Blackwell Publishing Ltd; Blackwell
• Subjects: Amino Acid Sequence; Biological and medical sciences; Calcium Signaling; Calreticulin - metabolism; Calreticulin - physiology; Endoplasmic Reticulum - metabolism; Fundamental and applied biological sciences. Psychology; Genes, Plant; Glycosylation; Molecular Sequence Data; Plant Development; Plant physiology and development; Plants - metabolism; Protein Folding; Protein Isoforms - metabolism; Protein Isoforms - physiology; Sequence Alignment; Stress, Physiological; Plant physiology; Calreticulin; Protein
• ISSN: 0031-9317; 1399-3054
• DOI: 10.1111/j.1399-3054.2009.01223.x

Calreticulin (CRT) is a key Ca²⁺-binding protein mainly resident in the endoplasmic reticulum (ER), which is highly conserved and extensively expressed in all eukaryotic organisms investigated. The protein plays important roles in a variety of cellular processes including Ca²⁺ signaling and protein folding. Although calreticulin has been well characterized in mammalian systems, increased investigations have demonstrated that plant CRTs have a number of specific properties different from their animal counterparts. Recent developments on plant CRTs have highlighted the significance of CRTs in plants growth and development as well as biotic and abiotic stress responses. There are at least two distinct groups of calreticulin isoforms in higher plants. Glycosylation of CRT was uniquely observed in plants. In this article, we will describe our current understanding of plant calreticulin gene family, protein structure, cellular localization, and diverse functions in plants. We also discuss the prospects of using this information for genetic improvements of crop plants.