{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fazeli E"],"funding":["Novo Nordisk Foundation","Aarhus Universitet"],"pagination":["111136"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12860930"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["302(2)"],"pubmed_abstract":["Growing evidence suggests that defects in endosomal recycling are a causal mechanism for Alzheimer's disease (AD). Sortilin-like receptor 1 (SORL1) is an endosomal sorting receptor that acts together with the retromer complex to facilitate shuttling of cargo from endosomes back to the trans-Golgi network or to the cell surface. Accumulating data indicate that SORL1 dysfunction contributes to AD pathogenesis. SORL1 is trafficked from the endosome to the cell surface in a retromer-dependent process, where it undergoes enzymatic cleavage, resulting in shedding of the SORL1 ectodomain (also known as soluble SORL1). We capitalized on this physiological process to develop and validate a cell-based luminescent reporter assay incorporating enhanced Gaussia luciferase (eGLuc) to quantify soluble SO"],"journal":["The Journal of biological chemistry"],"pubmed_title":["A luminescent reporter assay to quantify SORL1 ectodomain shedding and retromer-dependent endosome recycling activity."],"pmcid":["PMC12860930"],"funding_grant_id":["NNF20OC0064162"],"pubmed_authors":["Andersen OM","Huber AK","Fazeli E","Jan A","Jensen AMG","Merchant K","Klein J"],"additional_accession":[]},"is_claimable":false,"name":"A luminescent reporter assay to quantify SORL1 ectodomain shedding and retromer-dependent endosome recycling activity.","description":"Growing evidence suggests that defects in endosomal recycling are a causal mechanism for Alzheimer's disease (AD). Sortilin-like receptor 1 (SORL1) is an endosomal sorting receptor that acts together with the retromer complex to facilitate shuttling of cargo from endosomes back to the trans-Golgi network or to the cell surface. Accumulating data indicate that SORL1 dysfunction contributes to AD pathogenesis. SORL1 is trafficked from the endosome to the cell surface in a retromer-dependent process, where it undergoes enzymatic cleavage, resulting in shedding of the SORL1 ectodomain (also known as soluble SORL1). We capitalized on this physiological process to develop and validate a cell-based luminescent reporter assay incorporating enhanced Gaussia luciferase (eGLuc) to quantify soluble SO","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-07-14T17:19:19.966Z","creation":"2026-06-21T03:13:08.684Z"},"accession":"S-EPMC12860930","cross_references":{"pubmed":["41519200"],"doi":["10.1016/j.jbc.2026.111136"]}}