A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6.

@article{Okada2003ASP,
  title={A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6.},
  author={Tetsuya Okada and Kyosuke Haze and Satomi Nadanaka and Hiderou Yoshida and Nabil G Seidah and Yuko Mandai Hirano and Ryuichiro Sato and Manabu Negishi and Kazutoshi Mori},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 33},
  pages={31024-32}
}
Mammalian cells express several transcription factors embedded in the endoplasmic reticulum (ER) as transmembrane proteins that are activated by proteolysis, and two types of these proteins have been extensively investigated. One type comprises the sterol regulatory element-binding proteins (SREBP-1 and SREBP-2). The other type comprises the activating transcription factors 6 (ATF6alpha and ATF6beta), which are activated in response to ER stress. It was shown previously that both SREBP and ATF6… CONTINUE READING