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Although\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    is known to promote A\u03b2 pathology, recent data also support an effect of\u00a0\n                    <jats:italic>APOE<\/jats:italic>\n                    \u00a0polymorphism on phosphorylated Tau (pTau) pathology. To elucidate these potential effects, the pTau interactome was analyzed across\u00a0\n                    <jats:italic>APOE<\/jats:italic>\n                    \u00a0genotypes in the frontal cortex of 10 advanced AD cases (\n                    <jats:italic>n<\/jats:italic>\n                    \u2009=\u20095\u00a0\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\u03b53\/\u03b53<\/jats:sup>\n                    and\n                    <jats:italic>n<\/jats:italic>\n                    \u2009=\u20095\u00a0\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54\/\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    ), using a combination of anti-pTau pS396\/pS404 (PHF1) immunoprecipitation (IP) and mass spectrometry (MS). This proteomic approach was complemented by an analysis of anti-pTau PHF1 and anti-A\u03b2 4G8 immunohistochemistry, performed in the frontal cortex of 21 advanced AD cases (\n                    <jats:italic>n<\/jats:italic>\n                    \u2009=\u200911\u00a0\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\u03b53\/\u03b53<\/jats:sup>\n                    and\n                    <jats:italic>n<\/jats:italic>\n                    \u2009=\u200910\u00a0\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54\/\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    ). Our dataset includes 1130 and 1330 proteins enriched in IP\n                    <jats:sub>PHF1<\/jats:sub>\n                    samples from\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\u03b53\/\u03b53<\/jats:sup>\n                    and\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54\/\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    groups (fold change\u2009\u2265\u20091.50, IP\n                    <jats:sub>PHF1<\/jats:sub>\n                    <jats:italic>vs<\/jats:italic>\n                    IP\n                    <jats:sub>IgG ctrl<\/jats:sub>\n                    ). We identified 80 and 68 proteins as probable pTau interactors in\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\u03b53\/\u03b53<\/jats:sup>\n                    and\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54\/\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    groups, respectively (SAINT score\u2009\u2265\u20090.80; false discovery rate (FDR)\u2009\u2264\u20095%). A total of 47\/80 proteins were identified as more likely to interact with pTau in\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b53\/\u03b53<\/jats:italic>\n                    <\/jats:sup>\n                    <jats:italic>vs APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54\/\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    cases. Functional enrichment analyses showed that they were significantly associated with the nucleoplasm compartment and involved in RNA processing. In contrast, 35\/68 proteins were identified as more likely to interact with pTau in\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54\/\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    <jats:italic>vs APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b53\/\u03b53<\/jats:italic>\n                    <\/jats:sup>\n                    cases. They were significantly associated with the synaptic compartment and involved in cellular transport. A characterization of Tau pathology in the frontal cortex showed a higher density of plaque-associated neuritic crowns, made of dystrophic axons and synapses, in\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    carriers. Cerebral amyloid angiopathy was more frequent and severe in\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54\/\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    cases. Our study supports an influence of\n                    <jats:italic>APOE<\/jats:italic>\n                    genotype on pTau-subcellular location in AD. These results suggest a facilitation of pTau progression to A\u03b2-affected brain regions in\n                    <jats:italic>APOE<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b54<\/jats:italic>\n                    <\/jats:sup>\n                    carriers, paving the way to the identification of new therapeutic targets.\n                  <\/jats:p>","DOI":"10.1007\/s00401-024-02744-8","type":"journal-article","created":{"date-parts":[[2024,5,21]],"date-time":"2024-05-21T15:01:41Z","timestamp":1716303701000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["The influence of APOE\u03b54 on the pTau interactome in sporadic Alzheimer\u2019s disease"],"prefix":"10.1007","volume":"147","author":[{"given":"Manon","family":"Thierry","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jackeline","family":"Ponce","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mitchell","family":"Mart\u00e0-Ariza","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manor","family":"Askenazi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arline","family":"Faustin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominique","family":"Leitner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Geoffrey","family":"Pires","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evgeny","family":"Kanshin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eleanor","family":"Drummond","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beatrix","family":"Ueberheide","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3379-8966","authenticated-orcid":false,"given":"Thomas","family":"Wisniewski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,5,21]]},"reference":[{"key":"2744_CR1","doi-asserted-by":"publisher","first-page":"1680","DOI":"10.1038\/S41591-019-0611-3","volume":"25","author":"J Arboleda-Velasquez","year":"2019","unstructured":"Arboleda-Velasquez J, Lopera F, O\u2019Hare M, Delgado-Tirado S, Marino C, Chmielewska N et al (2019) Resistance to autosomal dominant Alzheimer\u2019s disease in an APOE3 Christchurch homozygote: a case report. 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