{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shi A"],"funding":["NIGMS NIH HHS"],"pagination":["1913-24"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2175126"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(22)"],"pubmed_abstract":["<h4>Background</h4>Alix/Bro1p family proteins have recently been identified as important components of multivesicular endosomes (MVEs) and are involved in the sorting of endocytosed integral membrane proteins, interacting with components of the ESCRT complex, the unconventional phospholipid LBPA, and other known endocytosis regulators. During infection, Alix can be co-opted by enveloped retroviruses, including HIV, providing an important function during virus budding from the plasma membrane. In addition, Alix is associated with the actin cytoskeleton and might regulate cytoskeletal dynamics.<h4>Results</h4>Here we demonstrate a novel physical interaction between the only apparent Alix/Bro1p family protein in C. elegans, ALX-1, and a key regulator of receptor recycling from endosomes to th"],"journal":["Current biology : CB"],"pubmed_title":["A novel requirement for C. elegans Alix/ALX-1 in RME-1-mediated membrane transport."],"pmcid":["PMC2175126"],"funding_grant_id":["R01 GM067237","R01 GM067237-05","GM67237"],"pubmed_authors":["Pant S","Grant BD","Shi A","Balklava Z","Chen CC","Figueroa V"],"additional_accession":[]},"is_claimable":false,"name":"A novel requirement for C. elegans Alix/ALX-1 in RME-1-mediated membrane transport.","description":"<h4>Background</h4>Alix/Bro1p family proteins have recently been identified as important components of multivesicular endosomes (MVEs) and are involved in the sorting of endocytosed integral membrane proteins, interacting with components of the ESCRT complex, the unconventional phospholipid LBPA, and other known endocytosis regulators. During infection, Alix can be co-opted by enveloped retroviruses, including HIV, providing an important function during virus budding from the plasma membrane. In addition, Alix is associated with the actin cytoskeleton and might regulate cytoskeletal dynamics.<h4>Results</h4>Here we demonstrate a novel physical interaction between the only apparent Alix/Bro1p family protein in C. elegans, ALX-1, and a key regulator of receptor recycling from endosomes to th","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Nov","modification":"2026-03-16T16:40:56.614Z","creation":"2019-03-27T02:22:25Z"},"accession":"S-EPMC2175126","cross_references":{"pubmed":["17997305"],"doi":["10.1016/j.cub.2007.10.045"]}}