{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bell TA"],"funding":["Helen Hay Whitney Foundation","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["e100061"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11405016"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["Prominin 1 (Prom1) is a five-transmembrane pass integral membrane protein that associates with curved regions of the plasma membrane. Prom1 interacts with membrane cholesterol and actively remodels the plasma membrane. Membrane-bending activity is particularly evident in photoreceptors, where Prom1 loss-of-function mutations cause failure of outer segment homeostasis, leading to cone-rod retinal dystrophy (CRRD). The Tweety Homology (Ttyh) protein family has been proposed to be homologous to Prominin, but it is not known whether Ttyh proteins have an analogous membrane-bending function. Here, we characterize the membrane-bending activity of human Prom1 and Ttyh1 in native bilayer membranes. We find that Prom1 and Ttyh1 both induce formation of extracellular vesicles (EVs) in cultured mamma"],"journal":["eLife"],"pubmed_title":["Prominin 1 and Tweety Homology 1 both induce extracellular vesicle formation."],"pmcid":["PMC11405016"],"funding_grant_id":["R35 GM142553","R35GM142553"],"pubmed_authors":["Monshizadeh A","Bell TA","Nguyen TH","Dardari H","Luce BE","Chao LH","Ananda VY","Hakim P"],"additional_accession":[]},"is_claimable":false,"name":"Prominin 1 and Tweety Homology 1 both induce extracellular vesicle formation.","description":"Prominin 1 (Prom1) is a five-transmembrane pass integral membrane protein that associates with curved regions of the plasma membrane. Prom1 interacts with membrane cholesterol and actively remodels the plasma membrane. Membrane-bending activity is particularly evident in photoreceptors, where Prom1 loss-of-function mutations cause failure of outer segment homeostasis, leading to cone-rod retinal dystrophy (CRRD). The Tweety Homology (Ttyh) protein family has been proposed to be homologous to Prominin, but it is not known whether Ttyh proteins have an analogous membrane-bending function. Here, we characterize the membrane-bending activity of human Prom1 and Ttyh1 in native bilayer membranes. We find that Prom1 and Ttyh1 both induce formation of extracellular vesicles (EVs) in cultured mamma","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-06-02T23:19:17.631Z","creation":"2025-04-04T01:18:13.35Z"},"accession":"S-EPMC11405016","cross_references":{"pubmed":["39136554"],"doi":["10.7554/eLife.100061"]}}