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000138760 0247_ $$2doi$$a10.1074/jbc.M116.741082
000138760 0247_ $$2pmid$$apmid:27432880
000138760 0247_ $$2pmc$$apmc:PMC5016686
000138760 0247_ $$2ISSN$$a0021-9258
000138760 0247_ $$2ISSN$$a1067-8816
000138760 0247_ $$2ISSN$$a1083-351X
000138760 037__ $$aDZNE-2020-05082
000138760 041__ $$aEnglish
000138760 082__ $$a540
000138760 1001_ $$0P:(DE-2719)2810826$$aOroz, Javier$$b0$$eFirst author$$udzne
000138760 245__ $$aASC Pyrin Domain Self-associates and Binds NLRP3 Protein Using Equivalent Binding Interfaces.
000138760 260__ $$aBethesda, Md.$$bSoc.60645$$c2016
000138760 264_1 $$2Crossref$$3online$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2016-07-18
000138760 264_1 $$2Crossref$$3print$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2016-09-09
000138760 3367_ $$2DRIVER$$aarticle
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000138760 3367_ $$2BibTeX$$aARTICLE
000138760 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000138760 3367_ $$00$$2EndNote$$aJournal Article
000138760 520__ $$aDeath domain superfamily members typically act as adaptors mediating in the assembly of supramolecular complexes with critical apoptosis and inflammation functions. These modular proteins consist of death domains, death effector domains, caspase recruitment domains, and pyrin domains (PYD). Despite the high structural similarity among them, only homotypic interactions participate in complex formation, suggesting that subtle factors differentiate each interaction type. It is thus critical to identify these factors as an essential step toward the understanding of the molecular basis of apoptosis and inflammation. The proteins apoptosis-associated speck-like protein containing a CARD (ASC) and NLRP3 play key roles in the regulation of apoptosis and inflammation through self-association and protein-protein interactions mediated by their PYDs. To better understand the molecular basis of their function, we have characterized ASC and NLRP3 PYD self-association and their intermolecular interaction by solution NMR spectroscopy and analytical ultracentrifugation. We found that ASC self-associates and binds NLRP3 PYD through equivalent protein regions, with higher binding affinity for the latter. These regions are located at opposite sides of the protein allowing multimeric complex formation previously shown in ASC PYD fibril assemblies. We show that NLRP3 PYD coexists in solution as a monomer and highly populated large-order oligomerized species. Despite this, we determined its monomeric three-dimensional solution structure by NMR and characterized its binding to ASC PYD. Using our novel structural data, we propose molecular models of ASC·ASC and ASC·NLRP3 PYD early supramolecular complexes, providing new insights into the molecular mechanisms of inflammasome and apoptosis signaling.
000138760 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000138760 650_7 $$2NLM Chemicals$$aCARD Signaling Adaptor Proteins
000138760 650_7 $$2NLM Chemicals$$aCytoskeletal Proteins
000138760 650_7 $$2NLM Chemicals$$aNLR Family, Pyrin Domain-Containing 3 Protein
000138760 650_7 $$2NLM Chemicals$$aNLRP3 protein, human
000138760 650_7 $$2NLM Chemicals$$aPYCARD protein, human
000138760 650_2 $$2MeSH$$aCARD Signaling Adaptor Proteins
000138760 650_2 $$2MeSH$$aCytoskeletal Proteins: chemistry
000138760 650_2 $$2MeSH$$aCytoskeletal Proteins: genetics
000138760 650_2 $$2MeSH$$aCytoskeletal Proteins: metabolism
000138760 650_2 $$2MeSH$$aHumans
000138760 650_2 $$2MeSH$$aModels, Molecular
000138760 650_2 $$2MeSH$$aNLR Family, Pyrin Domain-Containing 3 Protein: chemistry
000138760 650_2 $$2MeSH$$aNLR Family, Pyrin Domain-Containing 3 Protein: genetics
000138760 650_2 $$2MeSH$$aNLR Family, Pyrin Domain-Containing 3 Protein: metabolism
000138760 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000138760 650_2 $$2MeSH$$aProtein Binding
000138760 650_2 $$2MeSH$$aProtein Structure, Quaternary
000138760 650_2 $$2MeSH$$aPyrin Domain
000138760 650_2 $$2MeSH$$aUltracentrifugation
000138760 7001_ $$aBarrera-Vilarmau, Susana$$b1
000138760 7001_ $$aAlfonso, Carlos$$b2
000138760 7001_ $$aRivas, Germán$$b3
000138760 7001_ $$0P:(DE-HGF)0$$ade Alba, Eva$$b4$$eCorresponding author
000138760 77318 $$2Crossref$$3journal-article$$a10.1074/jbc.m116.741082$$b : American Society for Biochemistry & Molecular Biology (ASBMB), 2016-07-18$$n37$$p19487-19501$$tJournal of Biological Chemistry$$v291$$x0021-9258$$y2016
000138760 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M116.741082$$gVol. 291, no. 37, p. 19487 - 19501$$n37$$p19487-19501$$q291:37<19487 - 19501$$tThe journal of biological chemistry$$v291$$x0021-9258$$y2016
000138760 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC5016686
000138760 909CO $$ooai:pub.dzne.de:138760$$pVDB
000138760 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2810826$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b0$$kDZNE
000138760 9131_ $$0G:(DE-HGF)POF3-342$$1G:(DE-HGF)POF3-340$$2G:(DE-HGF)POF3-300$$aDE-HGF$$bForschungsbereich Gesundheit$$lErkrankungen des Nervensystems$$vDisease Mechanisms and Model Systems$$x0
000138760 9141_ $$y2016
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000138760 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bJ BIOL CHEM : 2017
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