Chaperones and foldases in endoplasmic reticulum stress signaling in plants

Gupta, Dinesh ; Tuteja, Narendra (2011) Chaperones and foldases in endoplasmic reticulum stress signaling in plants Plant Signaling & Behavior, 6 (2). pp. 232-236. ISSN 1559-2316

Full text not available from this repository.

Official URL: http://www.es.landesbioscience.com/journals/psb/ar...

Related URL: http://dx.doi.org/10.4161/psb.6.2.15490

Abstract

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), protein-disulfide isomerase (PDI), peptidyl-prolyl isomerases (PPI) or immunophilins, calnexin and calreticulin.

Item Type:Article
Source:Copyright of this article belongs to Landes Bioscience.
Keywords:Abiotic Stress; Chaperones; Endoplasmic Reticulum; Foldases; Immunophilins; Protein Folding; Signal Transduction
ID Code:52926
Deposited On:04 Aug 2011 12:06
Last Modified:04 Aug 2011 12:06

Repository Staff Only: item control page