ER-resident protein
From Proteopedia
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'''ER-resident proteins''' (ERp) are proteins which are retained by the endoplasmic reticulum<ref>PMID:21329881</ref>. | '''ER-resident proteins''' (ERp) are proteins which are retained by the endoplasmic reticulum<ref>PMID:21329881</ref>. | ||
*'''ERp18''' monitors control ensuring optimal processing of ATF6alpha following its trafficking to the Golgi<ref>PMID:31368601</ref>. | *'''ERp18''' monitors control ensuring optimal processing of ATF6alpha following its trafficking to the Golgi<ref>PMID:31368601</ref>. | ||
| + | *'''ERp27''' functions a a disulphide isomerase<ref>PMID:16940051</ref>. | ||
For details on ERdj5 see [[Molecular Playground/ERDj5]]. | For details on ERdj5 see [[Molecular Playground/ERDj5]]. | ||
Revision as of 07:59, 19 June 2024
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3D Structures of ER-resident protein
Updated on 19-June-2024
References
- ↑ Hagiwara M, Maegawa K, Suzuki M, Ushioda R, Araki K, Matsumoto Y, Hoseki J, Nagata K, Inaba K. Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5. Mol Cell. 2011 Feb 18;41(4):432-44. PMID:21329881 doi:10.1016/j.molcel.2011.01.021
- ↑ Oka OB, van Lith M, Rudolf J, Tungkum W, Pringle MA, Bulleid NJ. ERp18 regulates activation of ATF6α during unfolded protein response. EMBO J. 2019 Aug 1;38(15):e100990. PMID:31368601 doi:10.15252/embj.2018100990
- ↑ Alanen HI, Williamson RA, Howard MJ, Hatahet FS, Salo KE, Kauppila A, Kellokumpu S, Ruddock LW. ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57. J Biol Chem. 2006 Nov 3;281(44):33727-38. PMID:16940051 doi:10.1074/jbc.M604314200
