ATF6 (ATF6-alpha) activates chaperones

Stable Identifier
R-HSA-381033
Type
Pathway
Species
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
18048764 The role for endoplasmic reticulum stress in diabetes mellitus

Cardozo, AK, Eizirik, DL, Cnop, M

Endocr Rev 2008
25821458 Transcriptional regulation of secretory capacity by bZip transcription factors

Fox, RM, Andrew, DJ

Front Biol (Beijing) 2015
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

Kaufman, RJ, Scheuner, D

Endocr Rev 2008
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Orthologous Events
Cross References
GlyCosmos
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