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Mol. Life Sci."],"published-print":{"date-parts":[[2022,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>\n                      Loss of the Sortilin-related receptor 1 (\n                      <jats:italic>SORL1<\/jats:italic>\n                      ) gene seems to act as a causal event for Alzheimer\u2019s disease (AD). Recent studies have established that loss of\n                      <jats:italic>SORL1<\/jats:italic>\n                      , as well as mutations in autosomal dominant AD genes\n                      <jats:italic>APP<\/jats:italic>\n                      and\n                      <jats:italic>PSEN1\/2<\/jats:italic>\n                      , pathogenically converge by swelling early endosomes, AD\u2019s cytopathological hallmark. Acting together with the retromer trafficking complex,\n                      <jats:italic>SORL1<\/jats:italic>\n                      has been shown to regulate the recycling of the amyloid precursor protein (APP) out of the endosome, contributing to endosomal swelling and to APP misprocessing. We hypothesized that\n                      <jats:italic>SORL1<\/jats:italic>\n                      plays a broader role in neuronal endosomal recycling and used human induced pluripotent stem cell-derived neurons (hiPSC-Ns) to test this hypothesis. We examined endosomal recycling of three transmembrane proteins linked to AD pathophysiology: APP, the BDNF receptor Tropomyosin-related kinase B (TRKB), and the glutamate receptor subunit AMPA1 (GLUA1).\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      We used isogenic hiPSCs engineered to have\n                      <jats:italic>SORL1<\/jats:italic>\n                      depleted or to have enhanced\n                      <jats:italic>SORL1<\/jats:italic>\n                      expression. We differentiated neurons from these cell lines and mapped the trafficking of APP, TRKB and GLUA1 within the endosomal network using confocal microscopy. We also performed cell surface recycling and lysosomal degradation assays to assess the functionality of the endosomal network in both\n                      <jats:italic>SORL1<\/jats:italic>\n                      -depleted and -overexpressing neurons. The functional impact of GLUA1 recycling was determined by measuring synaptic activity. Finally, we analyzed alterations in gene expression in\n                      <jats:italic>SORL1<\/jats:italic>\n                      -depleted neurons using RNA sequencing.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      We find that as with APP, endosomal trafficking of GLUA1 and TRKB is impaired by loss of\n                      <jats:italic>SORL1<\/jats:italic>\n                      . We show that trafficking of all three cargoes to late endosomes and lysosomes is affected by manipulating SORL1 expression. We also show that depletion of\n                      <jats:italic>SORL1<\/jats:italic>\n                      significantly impacts the endosomal recycling pathway for APP and GLUA1 at the level of the recycling endosome and trafficking to the cell surface. This has a functional effect on neuronal activity as shown by multi-electrode array (MEA). Conversely, increased\n                      <jats:italic>SORL1<\/jats:italic>\n                      expression enhances endosomal recycling for APP and GLUA1. Our unbiased transcriptomic data further support\n                      <jats:italic>SORL1<\/jats:italic>\n                      \u2019s role in endosomal recycling. We observe altered expression networks that regulate cell surface trafficking and neurotrophic signaling in SORL1-depleted neurons.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>\n                      Collectively, and together with other recent observations, these findings suggest that one role for\n                      <jats:italic>SORL1<\/jats:italic>\n                      is to contribute to endosomal degradation and recycling pathways in neurons, a conclusion that has both pathogenic and therapeutic implications for Alzheimer\u2019s disease.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1007\/s00018-022-04182-9","type":"journal-article","created":{"date-parts":[[2022,2,28]],"date-time":"2022-02-28T05:02:51Z","timestamp":1646024571000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":127,"title":["The Alzheimer\u2019s gene SORL1 is a regulator of endosomal traffic and recycling in human neurons"],"prefix":"10.1007","volume":"79","author":[{"given":"Swati","family":"Mishra","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Allison","family":"Knupp","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcell P.","family":"Szabo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles A.","family":"Williams","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chizuru","family":"Kinoshita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dale W.","family":"Hailey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuliang","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olav M.","family":"Andersen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2106-0339","authenticated-orcid":false,"given":"Jessica E.","family":"Young","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2022,2,28]]},"reference":[{"key":"4182_CR1","doi-asserted-by":"publisher","first-page":"1300","DOI":"10.1038\/s41388-020-01604-5","volume":"40","author":"H Al-Akhrass","year":"2021","unstructured":"Al-Akhrass H, Conway JRW, Poulsen ASA, Paatero I, Kaivola J, Padzik A, Andersen OM, Ivaska J (2021) A feed-forward loop between SorLA and HER3 determines heregulin response and neratinib resistance. 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