title: Defects in endoplasmic reticulum-associated degradation (ERAD) increase selenate sensitivity in Arabidopsis.
abstract: Stress can impair protein folding in the endoplasmic reticulum (ER). Minimizing the accumulation of misfolded proteins in the ER is achieved by ER-associated degradation (ERAD), which involves the retrograde transport and proteasomal removal of aberrant proteins. Recently, the proteasome has been implicated in a selenium stress response. However, it remains unknown if selenium causes ER stress in plants similar to animals, and if ERAD is associated with optimal selenium tolerance. This deficiency was addressed by monitoring selenate-treated Arabidopsis plants with mutations in HRD1 and SeL1L, participants of ERAD. hrd1a/hrd1b and sel1l mutants treated with selenate demonstrate decreased tolerance and ER stress, as judged by BiP2 accumulation. The data indicate that optimal plant growth during selenate stress requires ERAD.
authors.affiliation: a Coastal Carolina University , Biology Department , Conway , South Carolina , USA.
authors.forename: Doug
authors.initials: D
authors.lastname: Van Hoewyk
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D060746:Endoplasmic Reticulum-Associated Degradation / Q000235:genetics / Q000502:physiology*; D018384:Oxidative Stress / Q000235:genetics / Q000502:physiology; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D017510:Protein Folding; D012643:Selenium / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D046988:Proteasome Endopeptidase Complex; D012643:Selenium
keywords: BiP2; ER; ERAD; UPR; oxidative stress; protein misfolding; selenium