NLRP3:SUGT1:HSP90 SUGT1:HSP90 SGT1:HSP90 binds inactive NLRP3 Authored: Jupe, S, 2010-04-22 Edited: Jupe, S, 2011-04-28 Pubmed17435760 Reactome Database ID Release 43873951 Reactome, http://www.reactome.org ReactomeREACT_75769 Reviewed: Kufer, TA, 2011-04-28 Reviewed: Rittinger, K, 2011-06-06 Reviewed: Wong, Edmond, 2011-06-06 SGT1 and HSP90 bind the NLRP3 (NALP3) LRR domain. Genetic studies in plants suggest a role for SGT1-HSP90 as co-chaperones of plant resistance (R) proteins, serving to maintain them in an inactive but signaling-competent state. R-protein activation is beleived to lead to dissociation of the SGT1-HSP90 complex. SGT1 and HSP90 are highly conserved, while R proteins are structurally related to mammalian NLRs. Human SGT1 and HSP90 were found to bind NLRP3. Knockdown of human SGT1 by small interfering RNA or chemical inhibition of HSP90 abrogated NLRP3 inflammasome activity, indicating that they are involved in regulation of NLRP3 inflammasome signaling (Mayor et al. 2007).