The endoplasmic reticulum stress signaling pathways in plants.
The unfolded protein response (UPR) is an evolutionarily conserved mechanism by which all eukaryotic cells preserve the homeostasis of the endoplasmic reticulum (ER) in the face of accumulation of unfolded proteins in the ER. Plants possess at least two signaling pathways specific for UPR. ER membrane-bound ER stress sensor/transducers, AtbZIP60 and AtbZIP28, are basic leucine zipper transcription factors that are activated by regulated intramembrane proteolysis systems and regulate transcription of the UPR genes. These signaling pathways play important roles not only in the UPR but also in other biological processes such as the response to pathogens and heat stress.
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University Gokasho, Uji, Kyoto, Japan. urade@kais.kyoto-u.ac.jp
Reiko
R
Urade
D029681:Arabidopsis Proteins / Q000502:physiology*; D050976:Basic-Leucine Zipper Transcription Factors / Q000502:physiology*; D004721:Endoplasmic Reticulum / Q000502:physiology*; D005656:Fungal Proteins / Q000502:physiology; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D017510:Protein Folding; D015398:Signal Transduction / Q000502:physiology*; D013312:Stress, Physiological / Q000502:physiology*
D029681:Arabidopsis Proteins; D050976:Basic-Leucine Zipper Transcription Factors; D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; C060153:KAR2 protein, yeast; C530495:bZIP28 protein, Arabidopsis; C533092:bZIP60 protein, Arabidopsis