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5olm

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Revision as of 07:28, 2 September 2020

TRIM21

Structural highlights

5olm is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	RING-type E3 ubiquitin transferase, with EC number 2.3.2.27
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RO52_HUMAN] E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2. Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of IRF3, hence attenuating type I interferon (IFN)-dependent immune responses (PubMed:26347139).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10]

Publication Abstract from PubMed

Cell surface Fc receptors activate inflammation and are tightly controlled to prevent autoimmunity. Antibodies also simulate potent immune signalling from inside the cell via the cytosolic antibody receptor TRIM21, but how this is regulated is unknown. Here we show that TRIM21 signalling is constitutively repressed by its B-Box domain and activated by phosphorylation. The B-Box occupies an E2 binding site on the catalytic RING domain by mimicking E2-E3 interactions, inhibiting TRIM21 ubiquitination and preventing immune activation. TRIM21 is derepressed by IKKbeta and TBK1 phosphorylation of an LxxIS motif in the RING domain, at the interface with the B-Box. Incorporation of phosphoserine or a phosphomimetic within this motif relieves B-Box inhibition, promoting E2 binding, RING catalysis, NF-kappaB activation and cytokine transcription upon infection with DNA or RNA viruses. These data explain how intracellular antibody signalling is regulated and reveal that the B-Box is a critical regulator of RING E3 ligase activity.

Intracellular antibody signalling is regulated by phosphorylation of the Fc receptor TRIM21.,Dickson C, Fletcher AJ, Vaysburd M, Yang JC, Mallery DL, Zeng J, Johnson CM, McLaughlin SH, Skehel M, Maslen S, Cruickshank J, Huguenin-Dezot N, Chin JW, Neuhaus D, James LC Elife. 2018 Apr 18;7. pii: 32660. doi: 10.7554/eLife.32660. PMID:29667579^[11]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wada K, Kamitani T. Autoantigen Ro52 is an E3 ubiquitin ligase. Biochem Biophys Res Commun. 2006 Jan 6;339(1):415-21. Epub 2005 Nov 14. PMID:16297862 doi:http://dx.doi.org/10.1016/j.bbrc.2005.11.029
↑ Wada K, Tanji K, Kamitani T. Oncogenic protein UnpEL/Usp4 deubiquitinates Ro52 by its isopeptidase activity. Biochem Biophys Res Commun. 2006 Jan 20;339(3):731-6. PMID:16316627 doi:10.1016/j.bbrc.2005.11.076
↑ Wada K, Kamitani T. UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself. Biochem Biophys Res Commun. 2006 Mar 31;342(1):253-8. Epub 2006 Feb 6. PMID:16472766 doi:10.1016/j.bbrc.2006.01.144
↑ Sabile A, Meyer AM, Wirbelauer C, Hess D, Kogel U, Scheffner M, Krek W. Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein. Mol Cell Biol. 2006 Aug;26(16):5994-6004. PMID:16880511 doi:http://dx.doi.org/10.1128/MCB.01630-05
↑ Takahata M, Bohgaki M, Tsukiyama T, Kondo T, Asaka M, Hatakeyama S. Ro52 functionally interacts with IgG1 and regulates its quality control via the ERAD system. Mol Immunol. 2008 Apr;45(7):2045-54. Epub 2007 Nov 26. PMID:18022694 doi:http://dx.doi.org/10.1016/j.molimm.2007.10.023
↑ Yamochi T, Ohnuma K, Hosono O, Tanaka H, Kanai Y, Morimoto C. SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity. Biochem Biophys Res Commun. 2008 May 23;370(1):195-9. doi:, 10.1016/j.bbrc.2008.03.075. Epub 2008 Mar 24. PMID:18361920 doi:http://dx.doi.org/10.1016/j.bbrc.2008.03.075
↑ Higgs R, Ni Gabhann J, Ben Larbi N, Breen EP, Fitzgerald KA, Jefferies CA. The E3 ubiquitin ligase Ro52 negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. J Immunol. 2008 Aug 1;181(3):1780-6. PMID:18641315
↑ Espinosa A, Oke V, Elfving A, Nyberg F, Covacu R, Wahren-Herlenius M. The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters the nucleus upon cellular exposure to nitric oxide. Exp Cell Res. 2008 Dec 10;314(20):3605-13. doi: 10.1016/j.yexcr.2008.09.011. Epub, 2008 Sep 25. PMID:18845142 doi:http://dx.doi.org/10.1016/j.yexcr.2008.09.011
↑ Wada K, Niida M, Tanaka M, Kamitani T. Ro52-mediated monoubiquitination of IKK{beta} down-regulates NF-{kappa}B signalling. J Biochem. 2009 Dec;146(6):821-32. doi: 10.1093/jb/mvp127. Epub 2009 Aug 12. PMID:19675099 doi:http://dx.doi.org/10.1093/jb/mvp127
↑ Kimura T, Jain A, Choi SW, Mandell MA, Schroder K, Johansen T, Deretic V. TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity. J Cell Biol. 2015 Sep 14;210(6):973-89. PMID:26347139 doi:http://dx.doi.org/10.1083/jcb.201503023
↑ Dickson C, Fletcher AJ, Vaysburd M, Yang JC, Mallery DL, Zeng J, Johnson CM, McLaughlin SH, Skehel M, Maslen S, Cruickshank J, Huguenin-Dezot N, Chin JW, Neuhaus D, James LC. Intracellular antibody signalling is regulated by phosphorylation of the Fc receptor TRIM21. Elife. 2018 Apr 18;7. pii: 32660. doi: 10.7554/eLife.32660. PMID:29667579 doi:http://dx.doi.org/10.7554/eLife.32660

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5olm"

Categories: Large Structures | RING-type E3 ubiquitin transferase | James, L C | Antibody | Antiviral protein

@@ Line 1: / Line 1: @@
 ==TRIM21==
-<StructureSection load='5olm' size='340' side='right' caption='[[5olm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='5olm' size='340' side='right'caption='[[5olm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5olm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OLM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OLM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5olm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OLM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OLM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5olm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5olm OCA], [http://pdbe.org/5olm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5olm RCSB], [http://www.ebi.ac.uk/pdbsum/5olm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5olm ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5olm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5olm OCA], [http://pdbe.org/5olm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5olm RCSB], [http://www.ebi.ac.uk/pdbsum/5olm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5olm ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5olm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: RING-type E3 ubiquitin transferase]]
 [[Category: James, L C]]
 [[Category: Antibody]]
 [[Category: Antiviral protein]]

5olm

From Proteopedia

Revision as of 07:28, 2 September 2020

TRIM21

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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