Characterisation of Arabidopsis calnexin 1 and calnexin 2 in the endoplasmic reticulum and at plasmodesmata

• Published in: Protoplasma Vol. 254; no. 1; pp. 125 - 136
• Main Authors: Liu, Danny Y. T., Smith, Penelope M. C., Barton, Deborah A., Day, David A., Overall, Robyn L.
• Format: Journal Article
• Language: English
• Published: Vienna Springer Vienna 01.01.2017; Springer Nature B.V
• Subjects: Arabidopsis - genetics; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Arabidopsis thaliana; Biomedical and Life Sciences; calcium; calnexin; Calnexin - genetics; Calnexin - metabolism; calreticulin; Cell Biology; endoplasmic reticulum; Endoplasmic Reticulum - metabolism; Gene Expression Regulation, Plant; gene overexpression; green fluorescent protein; Green Fluorescent Proteins - metabolism; ions; Life Sciences; mutants; Mutation - genetics; Original Article; Permeability; Plant Sciences; Plants, Genetically Modified; plasmodesmata; Plasmodesmata - metabolism; protein folding; Protein Transport; RNA, Messenger - genetics; RNA, Messenger - metabolism; tissues; transfer DNA; Zoology; Calreticulin; Plasmodesmata; Calnexin; Endoplasmic reticulum

Calnexin (CNX) is a highly conserved endoplasmic reticulum (ER) chaperone protein. Both calnexin and the homologous ER-lumenal protein, calreticulin, bind calcium ions and participate in protein folding. There are two calnexins in Arabidopsis thaliana , CNX1 and CNX2. GUS expression demonstrated tha...