Journal
PLANT SIGNALING & BEHAVIOR
Volume 6, Issue 2, Pages 232-236Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/psb.6.2.15490
Keywords
Abiotic stress; chaperones; endoplasmic reticulum; foldases; immunophilins; protein folding; signal transduction
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Funding
- Department of Biotechnology (DBT)
- Department of Science and Technology (DST), Government of India
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Molecular chaperones and foldases are a diverse group of proteins that in vivo bind to misfolded or unfolded proteins (non-native or unstable proteins) and play important role in their proper folding. Stress conditions compel altered and heightened chaperone and foldase expression activity in the endoplasmic reticulum (ER), which highlights the role of these proteins, due to which several of the proteins under these classes were identified as heat shock proteins. Different chaperones and foldases are active in different cellular compartment performing specific tasks. The review will discuss the role of ER chaperones and foldases under stress conditions, to maintain proper protein folding dynamics in the plant cells and recent advances in the field. The ER chaperones and foldases, which are described in article, are binding protein (BiP), glucose regulated protein (GRP94), proteindisulfide isomerase (PDI), peptidyl-prolyl isomerases (PPI) or immunophilins, calnexin and calreticulin.
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