Effects of phosphorylation on the NLRP3 inflammasome

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dc.contributor.authorSandall, Christina F.
dc.contributor.authorMacDonald, Justin Anthony
dc.date.accessioned2019-04-24T16:19:53Z
dc.date.available2019-04-24T16:19:53Z
dc.date.issued2019-03-05
dc.description.abstractThe pyrin domain containing Nod-like receptors (NLRPs) are a family of pattern recognition receptors known to regulate an array of immune signaling pathways. Emergent studies demonstrate the potential for regulatory control of inflammasome assembly by phosphorylation, notably NLRP3. Over a dozen phosphorylation sites have been identified for NLRP3 with many more suggested by phosphoproteomic studies of the NLRP family. Well-characterized NLRP3 phosphorylation events include Ser198 by c-Jun terminal kinase (JNK), Ser295 by protein kinase D (PKD) and/or protein kinase A (PKA), and Tyr861 by an unknown kinase but is dephosphorylated by protein tyrosine phosphatase non-receptor 22 (PTPN22). Since the PKA- and PKD-dependent phosphorylation of NLRP3 at Ser295 is best characterized, we provide detailed review of this aspect of NLRP3 regulation. Phosphorylation of Ser295 can attenuate ATPase activity as compared to its dephosphorylated counterpart, and this event is likely unique to NLRP3. In silico modeling of NLRP3 is useful in predicting how Ser295 phosphorylation might impact upon the structural topology of the ATP-binding domain to influence catalytic activity. It is important to gain as complete understanding as possible of the complex phosphorylation-mediated mechanisms of regulation for NLRP3 in part because of its involvement in many pathological processes.en_US
dc.description.grantingagencyCanadian Institutes of Health Research - Foundation Schemeen_US
dc.identifier.citationSandall, C. F., & MacDonald, J. A. (2019). Effects of phosphorylation on the NLRP3 inflammasome, 1-33. http://dx.doi.org/10.1016/j.abb.2019.02.020en_US
dc.identifier.doihttp://dx.doi.org/10.1016/j.abb.2019.02.020en_US
dc.identifier.grantnumberHealth Challenges in Chronic Disease Signature Initiative (#THC-13523)en_US
dc.identifier.urihttp://hdl.handle.net/1880/110193
dc.identifier.urihttps://doi.org/10.11575/PRISM/43839
dc.language.isoengen_US
dc.publisher.departmentBiochemistry & Molecular Biologyen_US
dc.publisher.facultyCumming School of Medicineen_US
dc.publisher.institutionUniversity of Calgaryen_US
dc.subjectnucleotide-binding domain and leucine rich repeat-containing receptoren_US
dc.subjectNLRen_US
dc.subjectNLRPen_US
dc.subjectNACHTen_US
dc.subjectinflammasomeen_US
dc.subjectphosphorylationen_US
dc.subjectcAMP-dependent protein kinase, PKAen_US
dc.subjectmolecular modelingen_US
dc.titleEffects of phosphorylation on the NLRP3 inflammasomeen_US
dc.typeunknown
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