Reactome | ATF6 (ATF6-alpha) activates chaperones

ATF6 (ATF6-alpha) activates chaperones

Stable Identifier

R-HSA-381033

Type

Pathway

Species

Homo sapiens

Compartment

cytosol, endoplasmic reticulum lumen, endoplasmic reticulum membrane, nucleoplasm

ReviewStatus

5/5

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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 Eizirik, DL, Cardozo, AK, 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 Scheuner, D, Kaufman, RJ	Endocr Rev	2008