Publication Date:
2019
Description:
〈sec〉〈st〉Synopsis〈/st〉〈p〉〈textbox textbox-type="graphic"〉〈p〉〈inline-fig〉〈/inline-fig〉〈/p〉〈/textbox〉〈/p〉
〈p〉The unfolded protein response (UPR) involves the activation of three independent but integrated pathways, through the endoplasmic reticulum (ER) stress sensors PERK, IRE1 and ATF6. In this study, ER-resident oxidoreductase ERp18 is shown to regulate ATF6α trafficking to the Golgi complex and cleavage in human cells. These results, suggest an additional layer of quality control and tuning of signalling responses under stress conditions.〈/p〉
〈p〉 〈l type="unord"〉〈li〉〈p〉ERp18 associates with ATF6α following stress and catalyses disulfide exchange.〈/p〉〈/li〉
〈li〉〈p〉ATF6α activation is attenuated in ERp18 knockout cells.〈/p〉〈/li〉
〈li〉〈p〉Loss of ERp18 results in faster ER-to-Golgi transport of ATF6α.〈/p〉〈/li〉
〈li〉〈p〉ERp18 optimises the proteolytic processing of ATF6α at the Golgi complex.〈/p〉〈/li〉〈/l〉 〈/p〉〈/sec〉
Print ISSN:
0261-4189
Electronic ISSN:
1460-2075
Topics:
Biology
,
Medicine
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