{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Deinhardt K"],"funding":["Wellcome Trust"],"pagination":["459-71"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2064241"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["174(3)"],"pubmed_abstract":["Ligand-receptor complexes are internalized by a variety of endocytic mechanisms. Some are initiated within clathrin-coated membranes, whereas others involve lipid microdomains of the plasma membrane. In neurons, where alternative targeting to short- or long-range trafficking routes underpins the differential processing of synaptic vesicle components and neurotrophin receptors, the mechanism giving access to the axonal retrograde pathway remains unknown. To investigate this sorting process, we examined the internalization of a tetanus neurotoxin fragment (TeNT HC), which shares axonal carriers with neurotrophins and their receptors. Previous studies have shown that the TeNT HC receptor, which comprises polysialogangliosides, resides in lipid microdomains. We demonstrate that TeNT HC interna"],"journal":["The Journal of cell biology"],"pubmed_title":["Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1."],"pmcid":["PMC2064241"],"funding_grant_id":["060349"],"pubmed_authors":["Deinhardt K","Hopkins CR","Berninghausen O","Willison HJ","Schiavo G"],"additional_accession":[]},"is_claimable":false,"name":"Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1.","description":"Ligand-receptor complexes are internalized by a variety of endocytic mechanisms. Some are initiated within clathrin-coated membranes, whereas others involve lipid microdomains of the plasma membrane. In neurons, where alternative targeting to short- or long-range trafficking routes underpins the differential processing of synaptic vesicle components and neurotrophin receptors, the mechanism giving access to the axonal retrograde pathway remains unknown. To investigate this sorting process, we examined the internalization of a tetanus neurotoxin fragment (TeNT HC), which shares axonal carriers with neurotrophins and their receptors. Previous studies have shown that the TeNT HC receptor, which comprises polysialogangliosides, resides in lipid microdomains. We demonstrate that TeNT HC interna","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Jul","modification":"2025-06-01T00:10:52.237Z","creation":"2025-06-01T00:10:52.237Z"},"accession":"S-EPMC2064241","cross_references":{"pubmed":["16880274"],"doi":["10.1083/jcb.200508170"]}}