title: Endoplasmic reticulum proteins quality control and the unfolded protein response: the regulative mechanism of organisms against stress injuries.
abstract: The endoplasmic reticulum is the cellular compartment in which secretory proteins are synthesized and folded. Perturbations of endoplasmic reticulum homeostasis lead to the accumulation of unfolded proteins. The activation of the unfolded protein response during endoplasmic reticulum stress transmits information about the status of protein folding to the cytosol and nucleus. The unfolded protein response leads to the upregulation of genes encoding endoplasmic reticulum chaperones, attenuation of translation, and initiation of the endoplasmic reticulum quality control system to restore endoplasmic reticulum homeostasis. When the unfolded protein response is insufficient to rebuild the steady state in endoplasmic reticulum, the programmed cell death or apoptosis would be initiated, by triggering cell injuries, even to cell death through apoptosis signals. In this review, we briefly outline research on the chaperones and foldases conserved in eukaryotes and plants, and describe the general principles and mechanisms of the endoplasmic reticulum quality control and the unfolded protein response. We describe the current models for the molecular mechanism of the unfolded protein response in plants, and emphasize the role of inositol requiring enzyme-1-dependent network in the unfolded protein response. Finally, we give a general overview of the directions for future research on the unfolded protein response in plants and its role in the response to environmental stresses.
authors.affiliation: Division of National Research Center for Apple Engineering and Technology, Shandong Agricultural University, Tai'an, Shandong, China; Division of State Key Laboratory of Crop Biology, Shandong Agricultural University, Tai'an, Shandong, China; College of Horticulture Science and Engineering, Shandong Agricultural University, Tai'an, Shandong, China.
authors.forename: Xi Ling
authors.initials: XL
authors.lastname: Fu
authors.forename: Dong Sheng
authors.initials: DS
authors.lastname: Gao
mesh_terms: D051702:Activating Transcription Factor 6 / Q000235:genetics / Q000378:metabolism; D017209:Apoptosis; D017360:Arabidopsis / Q000235:genetics* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D050976:Basic-Leucine Zipper Transcription Factors / Q000235:genetics / Q000378:metabolism; D037281:Calnexin / Q000235:genetics / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000235:genetics / Q000378:metabolism; D059865:Endoplasmic Reticulum Stress / Q000235:genetics*; D018506:Gene Expression Regulation, Plant; D006706:Homeostasis; D018832:Molecular Chaperones / Q000235:genetics* / Q000378:metabolism; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction; D056811:Unfolded Protein Response / Q000235:genetics*; D019892:eIF-2 Kinase / Q000235:genetics / Q000378:metabolism
chemical_list: D051702:Activating Transcription Factor 6; D029681:Arabidopsis Proteins; D050976:Basic-Leucine Zipper Transcription Factors; D037281:Calnexin; D018832:Molecular Chaperones; D011494:Protein Kinases; D019892:eIF-2 Kinase; C080351:CNX1 protein, Arabidopsis; C092535:Cnx protein, Arabidopsis; C530495:bZIP28 protein, Arabidopsis; C446528:Ire1-2 protein, Arabidopsis
keywords: ER associated degradation; apoptosis; endoplasmic reticulum; endoplasmic reticulum quality control; inositol requiring enzyme-1; programmed cell death; stress; unfolded protein response