Home > Publications Database > Unbiased proteomic profiling reveals the IP3R modulator AHCYL1/IRBIT as a novel interactor of microtubule-associated protein tau. > print

001     163729
005     20240320115522.0
024 7 _ |a 10.1016/j.jbc.2022.101774
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024 7 _ |a 0021-9258
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024 7 _ |a 1067-8816
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024 7 _ |a 1083-351X
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037 _ _ |a DZNE-2022-00468
041 _ _ |a English
082 _ _ |a 610
100 1 _ |a Wischhof, Lena
|0 P:(DE-2719)2811527
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245 _ _ |a Unbiased proteomic profiling reveals the IP3R modulator AHCYL1/IRBIT as a novel interactor of microtubule-associated protein tau.
260 _ _ |a Bethesda, MD.
|c 2022
|b American Soc. for Biochemistry and Molecular Biology
336 7 _ |a article
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336 7 _ |a ARTICLE
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500 _ _ |a (CC BY)
520 _ _ |a 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.
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542 _ _ |i 2022-04-01
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|u https://www.elsevier.com/tdm/userlicense/1.0/
542 _ _ |i 2022-02-22
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650 _ 7 |a Alzheimer’s disease
|2 Other
650 _ 7 |a SAH hydrolase–like protein 1 (AHCYL1/IRBIT)
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650 _ 7 |a autophagy
|2 Other
650 _ 7 |a human protein microarray
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650 _ 7 |a microtubule-associated protein tau
|2 Other
650 _ 2 |a Endoplasmic Reticulum: genetics
|2 MeSH
650 _ 2 |a Endoplasmic Reticulum: metabolism
|2 MeSH
650 _ 2 |a Gene Expression
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Lectins, C-Type: genetics
|2 MeSH
650 _ 2 |a Lectins, C-Type: metabolism
|2 MeSH
650 _ 2 |a Membrane Proteins: genetics
|2 MeSH
650 _ 2 |a Membrane Proteins: metabolism
|2 MeSH
650 _ 2 |a Protein Binding
|2 MeSH
650 _ 2 |a Proteomics
|2 MeSH
650 _ 2 |a tau Proteins: genetics
|2 MeSH
650 _ 2 |a tau Proteins: metabolism
|2 MeSH
700 1 _ |a Adhikari, Aasha
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|1 Kaniyappan
|p 39 -
|2 Crossref
|t Mol. Neurodegener.
|v 15
|y 2020
999 C 5 |a 10.1371/annotation/6a917a2e-df4a-4ad9-99bb-6aa7218b833e
|1 Reinhardt
|9 -- missing cx lookup --
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|v 8
|y 2013

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21