ER-resident protein

From Proteopedia

spinqualitylabelsall models Mouse ERp5 (PDB code 3apo) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function ER-resident proteins (ERp) are proteins which are retained by the endoplasmic reticulum[1]. ERp18 monitors control ensuring optimal processing of ATF6alpha following its trafficking to the Golgi[2]. ERp27 functions a a disulphide isomerase[3]. ERp29 facilitates processing and transport of proteins in the early secretary pathway[4]. ERp44 may be involved in the control of oxidative protein folding[5]. ERp46 regulates the mannose-trimming of misfiled glycoproteins and thus their degradation[6]. ERdj5 reduces disulfides in proteins to be dislocated to the cytosol for degradation[7]. For details on ERdj5 see Molecular Playground/ERDj5. Structural insights The .

3D Structures of ER-resident protein

Updated on 19-June-2024

References

1. ↑ 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
2. ↑ 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
3. ↑ 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
4. ↑ Zhang D, Richardson DR. Endoplasmic reticulum protein 29 (ERp29): An emerging role in cancer. Int J Biochem Cell Biol. 2011 Jan;43(1):33-6. PMID:20920593 doi:10.1016/j.biocel.2010.09.019
5. ↑ Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 2002 Feb 15;21(4):835-44. PMID:11847130 doi:http://dx.doi.org/10.1093/emboj/21.4.835
6. ↑ Yu S, Ito S, Wada I, Hosokawa N. ER-resident protein 46 (ERp46) triggers the mannose-trimming activity of ER degradation-enhancing α-mannosidase-like protein 3 (EDEM3). J Biol Chem. 2018 Jul 6;293(27):10663-10674. PMID:29784879 doi:10.1074/jbc.RA118.003129
7. ↑ Oka OB, Pringle MA, Schopp IM, Braakman I, Bulleid NJ. ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor. Mol Cell. 2013 Jun 27;50(6):793-804. doi: 10.1016/j.molcel.2013.05.014. Epub 2013, Jun 13. PMID:23769672 doi:http://dx.doi.org/10.1016/j.molcel.2013.05.014