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000163729 1001_ $$0P:(DE-2719)2811527$$aWischhof, Lena$$b0$$eFirst author$$udzne
000163729 245__ $$aUnbiased proteomic profiling reveals the IP3R modulator AHCYL1/IRBIT as a novel interactor of microtubule-associated protein tau.
000163729 260__ $$aBethesda, MD.$$bAmerican Soc. for Biochemistry and Molecular Biology$$c2022
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000163729 520__ $$aMicrotubule-associated protein tau is a naturally unfolded protein that can modulate a vast array of physiological processes through direct or indirect binding with molecular partners. Aberrant tau homeostasis has been implicated in the pathogenesis of several neurodegenerative disorders, including Alzheimer's disease. In this study, we performed an unbiased high-content protein profiling assay by incubating recombinant human tau on microarrays containing thousands of human polypeptides. Among the putative tau-binding partners, we identify SAH hydrolase-like protein 1/inositol 1,4,5-trisphosphate receptor (IP3R)-binding protein (AHCYL1/IRBIT), a member of the SAH hydrolase family and a previously described modulator of IP3R activity. Using coimmunoprecipitation assays, we show that endogenous as well as overexpressed tau can physically interact with AHCYL1/IRBIT in brain tissues and cultured cells. Proximity ligation assay experiments demonstrate that tau overexpression may modify the close localization of AHCYL1/IRBIT to IP3R at the endoplasmic reticulum. Together, our experimental evidence indicates that tau interacts with AHCYL1/IRBIT and potentially modulates AHCYL1/IRBIT function.
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000163729 542__ $$2Crossref$$i2022-04-01$$uhttps://www.elsevier.com/tdm/userlicense/1.0/
000163729 542__ $$2Crossref$$i2022-02-22$$uhttp://creativecommons.org/licenses/by/4.0/
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000163729 650_7 $$2Other$$aAlzheimer’s disease
000163729 650_7 $$2Other$$aSAH hydrolase–like protein 1 (AHCYL1/IRBIT)
000163729 650_7 $$2Other$$aautophagy
000163729 650_7 $$2Other$$ahuman protein microarray
000163729 650_7 $$2Other$$amicrotubule-associated protein tau
000163729 650_2 $$2MeSH$$aEndoplasmic Reticulum: genetics
000163729 650_2 $$2MeSH$$aEndoplasmic Reticulum: metabolism
000163729 650_2 $$2MeSH$$aGene Expression
000163729 650_2 $$2MeSH$$aHumans
000163729 650_2 $$2MeSH$$aLectins, C-Type: genetics
000163729 650_2 $$2MeSH$$aLectins, C-Type: metabolism
000163729 650_2 $$2MeSH$$aMembrane Proteins: genetics
000163729 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000163729 650_2 $$2MeSH$$aProtein Binding
000163729 650_2 $$2MeSH$$aProteomics
000163729 650_2 $$2MeSH$$atau Proteins: genetics
000163729 650_2 $$2MeSH$$atau Proteins: metabolism
000163729 7001_ $$0P:(DE-2719)9001341$$aAdhikari, Aasha$$b1$$udzne
000163729 7001_ $$0P:(DE-2719)9001754$$aMondal, Mrityunjoy$$b2$$udzne
000163729 7001_ $$0P:(DE-2719)2812207$$aMarsal Cots, Anais$$b3$$udzne
000163729 7001_ $$0P:(DE-2719)2810342$$aBiernat, Jacek$$b4$$udzne
000163729 7001_ $$0P:(DE-2719)2541658$$aMandelkow, Eva Maria$$b5$$udzne
000163729 7001_ $$0P:(DE-2719)2541671$$aMandelkow, Eckhard$$b6$$udzne
000163729 7001_ $$0P:(DE-2719)2289209$$aEhninger, Dan$$b7$$udzne
000163729 7001_ $$0P:(DE-2719)2010732$$aNicotera, Pierluigi$$b8$$udzne
000163729 7001_ $$0P:(DE-2719)2158358$$aBano, Daniele$$b9$$eLast author$$udzne
000163729 77318 $$2Crossref$$3journal-article$$a10.1016/j.jbc.2022.101774$$bElsevier BV$$d2022-04-01$$n4$$p101774$$tJournal of Biological Chemistry$$v298$$x0021-9258$$y2022
000163729 773__ $$0PERI:(DE-600)1474604-9$$a10.1016/j.jbc.2022.101774$$gVol. 298, no. 4, p. 101774 -$$n4$$p101774$$tThe journal of biological chemistry$$v298$$x0021-9258$$y2022
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