ATF6alpha optimizes long-term endoplasmic reticulum function to protect cells from chronic stress.

By Jun Wu, D. Rutkowski, M. Dubois, Jayanth Swathirajan, T. Saunders, Junying Wang, B. Song, Grace D.-Y. Yau, R. Kaufman. Developmental Cell, 2007

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Glaucoma (2018, neutral): “Extracellular recording can be performed over a wide frequency range (1 Hz–10 kHz) or may be band-pass filtered to reveal action potentials only [10].”
Protein quality control in the early secretory pathway (2008, background): “…problem, with important medical implications, is what turns an adaptive response (finalized to increase the ER folding capacity, as in the case in profes- sional secretory cells) into a mal-adaptive response that causes cell death (Lin et al, 2007; Rutkowski and Kaufman, 2007; Wu et al, 2007a).”
The impact of the unfolded protein response on human disease (2012, background): “The role of pATF6(N) in development is apparently minimal because mice lacking ATF6 are viable without significant abnormalities, although ATF6-null mice are exquisitely sensitive to ER stress (Wu et al., 2007; Yamamoto et al., 2010).”
Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, positive): “Interestingly, however, mice lacking ATF6α or ATF6β do not have a major phenotype, whereas the dual deficiency is lethal (Wu et al., 2007; Yamamoto et al., 2007).”
Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities (2008, background): “Known or suspected target genes of ATF6α include GRP78, PDI and ER degradation-enhancing α-mannosidase-like protein 1 (EDEM1), resulting in increased ER chaperone activity and degradation of misfolded protein”