{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Clarke AL"],"funding":["NIH HHS","NIGMS NIH HHS"],"pagination":["ar144"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9727795"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["33(14)"],"pubmed_abstract":["Membrane remodeling mediated by heteropolymeric filaments composed of ESCRT-III subunits is an essential process that occurs at a variety of organelles to maintain cellular homeostasis. Members of the evolutionarily conserved Lgd/CC2D1 protein family have been suggested to regulate ESCRT-III polymer assembly, although their specific roles, particularly in vivo, remain unclear. Using the <i>Caenorhabditis elegans</i> early embryo as a model system, we show that Lgd/CC2D1 localizes to endosomal membranes, and its loss impairs endolysosomal cargo sorting and degradation. At the ultrastructural level, the absence of Lgd/CC2D1 results in the accumulation of enlarged endosomal compartments that contain a reduced number of intralumenal vesicles (ILVs). However, unlike aberrant endosome morphology caused by depletion of other ESCRT components, ILV size is only modestly altered in embryos lacking Lgd/CC2D1. Instead, loss of Lgd/CC2D1 impairs normal accumulation of ESCRT-III on endosomal membranes, likely slowing the kinetics of ILV formation. Together, our findings suggest a role for Lgd/CC2D1 in the recruitment and/or stable assembly of ESCRT-III subunits on endosomal membranes to facilitate efficient ILV biogenesis."],"journal":["Molecular biology of the cell"],"pubmed_title":["Lgd regulates ESCRT-III complex accumulation at multivesicular endosomes to control intralumenal vesicle formation."],"pmcid":["PMC9727795"],"funding_grant_id":["S10 OD026769","R35 GM134865"],"pubmed_authors":["Clarke AL","Lettman MM","Audhya A"],"additional_accession":[]},"is_claimable":false,"name":"Lgd regulates ESCRT-III complex accumulation at multivesicular endosomes to control intralumenal vesicle formation.","description":"Membrane remodeling mediated by heteropolymeric filaments composed of ESCRT-III subunits is an essential process that occurs at a variety of organelles to maintain cellular homeostasis. Members of the evolutionarily conserved Lgd/CC2D1 protein family have been suggested to regulate ESCRT-III polymer assembly, although their specific roles, particularly in vivo, remain unclear. Using the <i>Caenorhabditis elegans</i> early embryo as a model system, we show that Lgd/CC2D1 localizes to endosomal membranes, and its loss impairs endolysosomal cargo sorting and degradation. At the ultrastructural level, the absence of Lgd/CC2D1 results in the accumulation of enlarged endosomal compartments that contain a reduced number of intralumenal vesicles (ILVs). However, unlike aberrant endosome morphology caused by depletion of other ESCRT components, ILV size is only modestly altered in embryos lacking Lgd/CC2D1. Instead, loss of Lgd/CC2D1 impairs normal accumulation of ESCRT-III on endosomal membranes, likely slowing the kinetics of ILV formation. Together, our findings suggest a role for Lgd/CC2D1 in the recruitment and/or stable assembly of ESCRT-III subunits on endosomal membranes to facilitate efficient ILV biogenesis.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-06T19:15:39.869Z","creation":"2025-04-06T19:15:39.869Z"},"accession":"S-EPMC9727795","cross_references":{"pubmed":["36287829"],"doi":["10.1091/mbc.E22-08-0342"]}}