<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Bell TA</submitter><funding>Helen Hay Whitney Foundation</funding><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><pagination>e100061</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11405016</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13</volume><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</pubmed_abstract><journal>eLife</journal><pubmed_title>Prominin 1 and Tweety Homology 1 both induce extracellular vesicle formation.</pubmed_title><pmcid>PMC11405016</pmcid><funding_grant_id>R35 GM142553</funding_grant_id><funding_grant_id>R35GM142553</funding_grant_id><pubmed_authors>Monshizadeh A</pubmed_authors><pubmed_authors>Bell TA</pubmed_authors><pubmed_authors>Nguyen TH</pubmed_authors><pubmed_authors>Dardari H</pubmed_authors><pubmed_authors>Luce BE</pubmed_authors><pubmed_authors>Chao LH</pubmed_authors><pubmed_authors>Ananda VY</pubmed_authors><pubmed_authors>Hakim P</pubmed_authors></additional><is_claimable>false</is_claimable><name>Prominin 1 and Tweety Homology 1 both induce extracellular vesicle formation.</name><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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Aug</publication><modification>2026-06-02T23:19:17.631Z</modification><creation>2025-04-04T01:18:13.35Z</creation></dates><accession>S-EPMC11405016</accession><cross_references><pubmed>39136554</pubmed><doi>10.7554/eLife.100061</doi></cross_references></HashMap>