{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Solinger JA"],"funding":["Swiss National Science Foundation","Universität Basel","NIH HHS"],"pagination":["213-224"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7616953"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(2)"],"pubmed_abstract":["Endosomal transport is essential for cellular organization and compartmentalization and cell-cell communication. Sorting endosomes provide a crossroads for various trafficking pathways and determine recycling, secretion or degradation of proteins. The organization of these processes requires membrane-tethering factors to coordinate Rab GTPase function with membrane fusion. Here, we report a conserved tethering platform that acts in the Rab11 recycling pathways at sorting endosomes, which we name factors for endosome recycling and Rab interactions (FERARI). The Rab-binding module of FERARI consists of Rab11FIP5 and rabenosyn-5/RABS-5, while the SNARE-interacting module comprises VPS45 and VIPAS39. Unexpectedly, the membrane fission protein EHD1 is also a FERARI component. Thus, FERARI appears to combine fusion activity through the SM protein VPS45 with pinching activity through EHD1 on SNX-1-positive endosomal membranes. We propose that coordination of fusion and pinching through a kiss-and-run mechanism drives cargo at endosomes into recycling pathways."],"journal":["Nature cell biology"],"pubmed_title":["FERARI is required for Rab11-dependent endocytic recycling."],"pmcid":["PMC7616953"],"funding_grant_id":["CRSII3_141956","141207","P40 OD010440","141956","31003A_141207"],"pubmed_authors":["Spang A","Prescianotto-Baschong C","Solinger JA","Rashid HO"],"additional_accession":[]},"is_claimable":false,"name":"FERARI is required for Rab11-dependent endocytic recycling.","description":"Endosomal transport is essential for cellular organization and compartmentalization and cell-cell communication. Sorting endosomes provide a crossroads for various trafficking pathways and determine recycling, secretion or degradation of proteins. The organization of these processes requires membrane-tethering factors to coordinate Rab GTPase function with membrane fusion. Here, we report a conserved tethering platform that acts in the Rab11 recycling pathways at sorting endosomes, which we name factors for endosome recycling and Rab interactions (FERARI). The Rab-binding module of FERARI consists of Rab11FIP5 and rabenosyn-5/RABS-5, while the SNARE-interacting module comprises VPS45 and VIPAS39. Unexpectedly, the membrane fission protein EHD1 is also a FERARI component. Thus, FERARI appears to combine fusion activity through the SM protein VPS45 with pinching activity through EHD1 on SNX-1-positive endosomal membranes. We propose that coordination of fusion and pinching through a kiss-and-run mechanism drives cargo at endosomes into recycling pathways.","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Feb","modification":"2025-04-27T01:58:23.208Z","creation":"2025-04-06T18:24:15.22Z"},"accession":"S-EPMC7616953","cross_references":{"pubmed":["31988382"],"doi":["10.1038/s41556-019-0456-5"]}}