ATF6 (ATF6-alpha) activates chaperones

Stable Identifier
Homo sapiens
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ATF6-alpha is a transmembrane protein that normally resides in the Endoplasmic Reticulum (ER) membrane. Here its luminal C-terminal domain is associated with BiP, shielding 2 Golgi-targeting regions and thus keeping ATF6-alpha in the ER. Upon interaction of BiP with unfolded proteins in the ER, ATF6-alpha dissociates and transits to the Golgi where it is cleaved by the S1P and S2P proteases that reside in the Golgi, releasing the N-terminal domain of ATF6-alpha into the cytosol. After transiting to the nucleus, the N-terminal domain acts as a transcription factor to activate genes encoding chaperones.

Literature References
PubMed ID Title Journal Year
25821458 Transcriptional regulation of secretory capacity by bZip transcription factors

Fox, RM, Andrew, DJ

Front Biol (Beijing) 2015
18048764 The role for endoplasmic reticulum stress in diabetes mellitus

Eizirik, DL, Cardozo, AK, Cnop, M

Endocr Rev 2008
18038217 Endoplasmic reticulum stress responses

Schröder, M

Cell Mol Life Sci 2008
18436705 The unfolded protein response: a pathway that links insulin demand with beta-cell failure and diabetes

Scheuner, D, Kaufman, RJ

Endocr Rev 2008
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Event Information
Orthologous Events