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@ARTICLE{Wischhof:163729,
      author       = {Wischhof, Lena and Adhikari, Aasha and Mondal, Mrityunjoy
                      and Marsal Cots, Anais and Biernat, Jacek and Mandelkow, Eva
                      Maria and Mandelkow, Eckhard and Ehninger, Dan and Nicotera,
                      Pierluigi and Bano, Daniele},
      title        = {{U}nbiased proteomic profiling reveals the {IP}3{R}
                      modulator {AHCYL}1/{IRBIT} as a novel interactor of
                      microtubule-associated protein tau.},
      journal      = {The journal of biological chemistry},
      volume       = {298},
      number       = {4},
      issn         = {0021-9258},
      address      = {Bethesda, MD.},
      publisher    = {American Soc. for Biochemistry and Molecular Biology},
      reportid     = {DZNE-2022-00468},
      pages        = {101774},
      year         = {2022},
      note         = {(CC BY)},
      abstract     = {Microtubule-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.},
      keywords     = {Endoplasmic Reticulum: genetics / Endoplasmic Reticulum:
                      metabolism / Gene Expression / Humans / Lectins, C-Type:
                      genetics / Lectins, C-Type: metabolism / Membrane Proteins:
                      genetics / Membrane Proteins: metabolism / Protein Binding /
                      Proteomics / tau Proteins: genetics / tau Proteins:
                      metabolism / Alzheimer’s disease (Other) / SAH
                      hydrolase–like protein 1 (AHCYL1/IRBIT) (Other) /
                      autophagy (Other) / human protein microarray (Other) /
                      microtubule-associated protein tau (Other)},
      cin          = {AG Bano / AG Mandelkow 1 / AG Mandelkow 2 / AG Ehninger /
                      Scientific board},
      ddc          = {610},
      cid          = {I:(DE-2719)1013003 / I:(DE-2719)1013014 /
                      I:(DE-2719)1013015 / I:(DE-2719)1013005 /
                      I:(DE-2719)1030000},
      pnm          = {351 - Brain Function (POF4-351) / 352 - Disease Mechanisms
                      (POF4-352)},
      pid          = {G:(DE-HGF)POF4-351 / G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35218773},
      pmc          = {pmc:PMC8956953},
      doi          = {10.1016/j.jbc.2022.101774},
      url          = {https://pub.dzne.de/record/163729},
}