{"doi":"10.1073/pnas.96.9.5013","title":"ADP-ribosylation factor 1 dependent clathrin-coat assembly on synthetic liposomes","abstract":"<jats:p>\n            The assembly of clathrin-coated vesicles on Golgi membranes is initiated by the GTP-binding protein ADP ribosylation factor (ARF), which generates high-affinity membrane-binding sites for the heterotetrameric AP-1 adaptor complex. Once bound, the AP-1 recruits clathrin triskelia, which polymerize to form the coat. We have found that ARF⋅GTP also recruits AP-1 and clathrin onto protein-free liposomes. The efficiency of this process is modulated by the composition of the liposomes, with phosphatidylserine being the most stimulatory phospholipid. There is also a requirement for cytosolic factor(s) other than ARF. Thin-section electron microscopy shows the presence of clathrin-coated buds and vesicles that resemble those formed\n            <jats:italic>in vivo</jats:italic>\n            . These results indicate that AP-1-containing clathrin-coated vesicles can form in the absence of integral membrane proteins. Thus, ARF⋅GTP, appropriate lipids, and cytosolic factor(s) are the minimal components necessary for AP-1 clathrin-coat assembly.\n          </jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1999,"id":24632,"datarank":3.681710633808523,"base_score":4.304065093204169,"endowment":4.304065093204169,"self_citation_contribution":0.6456097639806255,"citation_network_contribution":3.0361008698278975,"self_endowment_contribution":0.6456097639806255,"citer_contribution":3.0361008698278975,"corpus_percentile":null,"corpus_rank":null,"citation_count":73,"citer_count":70,"citers_with_citation_signal":61,"citers_with_endowment":61,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":147255,"name":"Matthew T. 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