ER-resident protein
From Proteopedia
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== Function == | == Function == | ||
| - | '''ER-resident proteins''' (ERp) are proteins which are retained by the endoplasmic reticulum<ref>PMID:21329881</ref>. For details on ERdj5 see [[Molecular Playground/ERDj5]]. | + | '''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>. | ||
| + | *'''ERp27''' functions a a disulphide isomerase<ref>PMID:16940051</ref>. | ||
| + | *'''ERp29''' facilitates processing and transport of proteins in the early secretary pathway<ref>PMID:20920593</ref>. | ||
| + | *'''ERp44''' may be involved in the control of oxidative protein folding<ref>PMID:11847130</ref>. | ||
| + | *'''ERp46''' regulates the mannose-trimming of misfiled glycoproteins and thus their degradation<ref>PMID:29784879</ref>. | ||
| + | *'''ERdj5''' reduces disulfides in proteins to be dislocated to the cytosol for degradation<ref>PMID:23769672</ref>. For details on ERdj5 see [[Molecular Playground/ERDj5]]. | ||
== Structural insights == | == Structural insights == | ||
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| + | *ERp18 or thioredoxin domain-containing protein 12 | ||
| + | |||
| + | **[[2k8v]] – hERp18 24-172 – human NMR<br /> | ||
*ERp27 | *ERp27 | ||
| - | **[[2l4c]] – hERp27 B domain | + | **[[2l4c]] – hERp27 B domain - NMR<br /> |
**[[4f9z]] – hERp27 tryptic domain <br /> | **[[4f9z]] – hERp27 tryptic domain <br /> | ||
| - | *ERp44 | + | *ERp29 |
| + | |||
| + | **[[2qc7]] – hERp29 <br /> | ||
| + | **[[5v8z]] – hERp29 D domain + calmegin P domain<br /> | ||
| + | **[[5v90]] – hERp29 D domain + calreticulin P domain<br /> | ||
| + | **[[2m66]], [[6o6i]] – rERp29 C terminal – rat - NMR<br /> | ||
| + | **[[1g7d]] – rERp29 C domain - NMR<br /> | ||
| + | **[[1g7e]] – rERp29 N domain - NMR<br /> | ||
| + | |||
| + | *ERp44 or thioredoxin domain-containing protein 4 | ||
| + | |||
| + | **[[[2r2j]], [5hqp]] – hERp44 + peroxiredoxin-4<br /> | ||
| - | * | + | *ERp46 or thioredoxin domain-containing protein 5 |
| - | + | ||
| - | * | + | **[[3uj1]], [[3uvt]] – hERp46 3rd catalytic domain 323-428 <br /> |
| + | **[[3wgd]] – hERp46 1st catalytic domain 62-170<br /> | ||
| + | **[[3wge]] – hERp46 2nd catalytic domain 190-298<br /> | ||
| + | **[[3wgx]] – hERp46 2nd catalytic domain + peroxiredoxin-4<br /> | ||
| - | **[[3uvt]] – hERp46 catalytic domain 3 <br /> | ||
| - | **[[3uj1]] – hERp46 thioredoxin 3 domain <br /> | ||
*ERdj5 | *ERdj5 | ||
Current revision
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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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
