Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface
about
SGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradationBag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domainUSP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradationStructural and Functional Insights into Small, Glutamine-Rich, Tetratricopeptide Repeat Protein AlphaHow Polyomaviruses Exploit the ERAD Machinery to Cause InfectionStructure of the Sgt2 dimerization domain complexed with the Get5 UBL domain involved in the targeting of tail-anchored membrane proteins to the endoplasmic reticulumSolution structure of the SGTA dimerisation domain and investigation of its interactions with the ubiquitin-like domains of BAG6 and UBL4ACanine REIC/Dkk-3 interacts with SGTA and restores androgen receptor signalling in androgen-independent prostate cancer cell lines.Differential gradients of interaction affinities drive efficient targeting and recycling in the GET pathwayThe association of BAG6 with SGTA and tail-anchored proteinsUbiquitin-like domains can target to the proteasome but proteolysis requires a disordered region.A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradationBag6/Bat3/Scythe: a novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation.SGTA: a new player in the molecular co-chaperone game.SGTA-Dependent Regulation of Hsc70 Promotes Cytosol Entry of Simian Virus 40 from the Endoplasmic Reticulum.The canine prostate cancer cell line CHP-1 shows over-expression of the co-chaperone small glutamine-rich tetratricopeptide repeat-containing protein α.Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis.Tumor suppressor REIC/DKK-3 and co-chaperone SGTA: Their interaction and roles in the androgen sensitivity.Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo.A conserved island of BAG6/Scythe is related to ubiquitin domains and participates in short hydrophobicity recognition.Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes.Multiple selection filters ensure accurate tail-anchored membrane protein targeting.Structural and functional insights into the E3 ligase, RNF126.SGTA regulates the cytosolic quality control of hydrophobic substrates.Mechanistic basis for a molecular triage reactionSGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism.Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.Binding of SGTA to Rpn13 selectively modulates protein quality control.Multiple pathways facilitate the biogenesis of mammalian tail-anchored proteins.
P2860
Q24306367-77485D63-76A9-4E46-BCB8-C3F9E572D59DQ24311324-49728BC6-5B77-4A35-B680-05880B589A0FQ24320201-3DFA77DF-3247-4207-938E-44CB876120FDQ26770509-453F16FA-1CB5-4479-B705-DA457A169B47Q27468807-6F50BAF2-02AB-4706-82DE-F5D171B5FA10Q27686994-15329A1E-F5CF-4D2F-9F1E-E599B787DA90Q28545114-20DC3B13-AB20-4D7C-BAB2-45E516D7C153Q33785251-0C2E8E0F-E147-42E2-8839-EF278E6A686BQ34581057-F726E571-BC1A-403A-9042-91D2A9EA3706Q34637885-6F40BBE4-887C-43BF-A3D4-45F3CC8E36E6Q36946185-C7128B32-FEAD-4002-B813-74A5A652F705Q36947746-276D3856-3023-4BB8-B051-242AE2A296C2Q38082449-092FFE38-0EC0-4062-BB27-CEB68C0DC124Q38118665-33C94F73-D1F8-4B52-9D26-8B642F620B13Q38709698-33F2DDBA-2660-4542-8F52-1B988D2CD04AQ38804028-A66C236E-3E6D-4F80-8C76-660F7A63BACCQ39474998-66DE0AF8-A60B-42DB-9080-46919A3AF57AQ39925769-B0E0F626-B98E-4C5D-BFBF-ED7F42705B02Q40031008-8E6326CB-1933-459A-B449-51FC65D056B1Q40215164-B9568D98-00C6-42DD-B632-AD40F803350BQ40530080-DD264654-83E8-45F4-939A-6CDDEC3F5273Q40778656-6A7B6734-EFB2-4CA7-8A4E-F93FCF9853B3Q42011073-843A7315-A116-4D85-A82A-4326FBC7EE7AQ42186480-DA1D4B65-8047-4A3A-894C-187195E79E50Q42292851-7C321B44-23C7-44D1-8855-F005F883C86CQ42371745-D9F8CE01-7426-4BC1-B05E-2185F5B048E9Q42700283-D4F2BB79-B392-42E4-BD29-4018F7494BD5Q43240834-33E68B04-E92B-450C-9594-8F9D93103D1DQ47108141-7DC634D1-DCB8-4D89-83FD-74487FEF0799
P2860
Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface
description
2012 nî lūn-bûn
@nan
2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@ast
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@en
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@nl
type
label
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@ast
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@en
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@nl
prefLabel
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@ast
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@en
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@nl
P2860
P3181
P1433
P1476
Structures of the Sgt2/SGTA Di ...... a Conserved Dynamic Interface
@en
P2093
David G VanderVelde
P2860
P304
P3181
P356
10.1016/J.CELREP.2012.10.010
P577
2012-12-27T00:00:00Z