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However, the role of Tau pathology in microglia activation or their causal relationship remains largely elusive.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>The levels of nucleotide\u2010binding oligomerisation domain\u00a0(NOD)\u2010like receptor pyrin domain containing 3\u00a0(NLRP3) acetylation and inflammasome activation in multiple cell models with Tau proteins treatment, transgenic mice with Tauopathy, and AD patients were measured by Western blotting and enzyme\u2010linked immunosorbent assay. In addition, the acetyltransferase activity of Tau and NLRP3 acetylation sites were confirmed using the test\u2010tube acetylation assay, co\u2010immunoprecipitation, immunofluorescence (IF) staining, mass spectrometry and molecular docking. The Tau\u2010overexpressing mouse model was established by overexpression of human Tau proteins in mouse hippocampal CA1 neurons through the adeno\u2010associated virus injection. The cognitive functions of Tau\u2010overexpressing mice were assessed in various behavioural tests, and microglia activation was analysed by Iba\u20101 IF staining and [18F]\u2010DPA\u2010714 positron emission tomography\/computed tomography imaging. A peptide that blocks the interaction between Tau and NLRP3 was synthesised to determine the in vitro and in vivo effects of Tau\u2013NLRP3 interaction blockade on NLRP3 acetylation, inflammasome activation, microglia activation and cognitive function.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>Excessively elevated NLRP3 acetylation and inflammasome activation were observed in 3xTg\u2010AD mice, microtubule\u2010associated protein Tau P301S (PS19) mice and AD patients. It was further confirmed that mimics of \u2018early\u2019 phosphorylated\u2010Tau proteins which increase at the initial stage of diseases with Tauopathy, including TauT181E, TauS199E, TauT217E and TauS262E, significantly promoted Tau\u2013K18 domain acetyltransferase activity\u2010dependent NLRP3 acetylation and inflammasome activation in HEK293T and BV\u20102 microglial cells. In addition, Tau protein could directly acetylate NLRP3 at the K21, K22 and K24 sites at its PYD domain and thereby induce inflammasome activation in vitro. Overexpression of human Tau proteins in mouse hippocampal CA1 neurons resulted in impaired cognitive function, Tau transmission to microglia and microgliosis with NLRP3 acetylation and inflammasome activation. As a targeted intervention, competitive binding of a designed Tau\u2013NLRP3\u2010binding blocking (TNB) peptide to block the interaction of Tau protein with NLRP3 inhibited the NLRP3 acetylation and downstream inflammasome activation in microglia, thereby alleviating microglia activation and cognitive impairment in mice.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>In conclusion, our findings provide evidence for a novel role of Tau in the regulation of microglia activation through acetylating NLRP3, which has potential implications for early intervention and personalised treatment of AD and related Tauopathies.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1002\/ctm2.1623","type":"journal-article","created":{"date-parts":[[2024,3,16]],"date-time":"2024-03-16T02:43:54Z","timestamp":1710557034000},"source":"Crossref","is-referenced-by-count":52,"title":["Tau induces 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