{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lucken-Ardjomande Hasler S"],"funding":["Swiss National Science Foundation","Medical Research Council"],"pagination":["e201811014"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7199855"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["219(5)"],"pubmed_abstract":["In addition to the classical pathway of secretion, some transmembrane proteins reach the plasma membrane through alternative routes. Several proteins transit through endosomes and are exported in a Rab8-, Rab10-, and/or Rab11-dependent manner. GRAFs are membrane-binding proteins associated with tubules and vesicles. We found extensive colocalization of GRAF1b/2 with Rab8a/b and partial with Rab10. We identified MICAL1 and WDR44 as direct GRAF-binding partners. MICAL1 links GRAF1b/2 to Rab8a/b and Rab10, and WDR44 binds Rab11. Endogenous WDR44 labels a subset of tubular endosomes, which are closely aligned with the ER via binding to VAPA/B. With its BAR domain, GRAF2 can tubulate membranes, and in its absence WDR44 tubules are not observed. We show that GRAF2 and WDR44 are essential for the"],"journal":["The Journal of cell biology"],"pubmed_title":["GRAF2, WDR44, and MICAL1 mediate Rab8/10/11-dependent export of E-cadherin, MMP14, and CFTR ΔF508."],"pmcid":["PMC7199855"],"funding_grant_id":["PA00P3-124164","PBGE1-121206","MC_U105178795","U105178795"],"pubmed_authors":["Pasche M","Lucken-Ardjomande Hasler S","McMahon HT","Vallis Y"],"additional_accession":[]},"is_claimable":false,"name":"GRAF2, WDR44, and MICAL1 mediate Rab8/10/11-dependent export of E-cadherin, MMP14, and CFTR ΔF508.","description":"In addition to the classical pathway of secretion, some transmembrane proteins reach the plasma membrane through alternative routes. Several proteins transit through endosomes and are exported in a Rab8-, Rab10-, and/or Rab11-dependent manner. GRAFs are membrane-binding proteins associated with tubules and vesicles. We found extensive colocalization of GRAF1b/2 with Rab8a/b and partial with Rab10. We identified MICAL1 and WDR44 as direct GRAF-binding partners. MICAL1 links GRAF1b/2 to Rab8a/b and Rab10, and WDR44 binds Rab11. Endogenous WDR44 labels a subset of tubular endosomes, which are closely aligned with the ER via binding to VAPA/B. With its BAR domain, GRAF2 can tubulate membranes, and in its absence WDR44 tubules are not observed. We show that GRAF2 and WDR44 are essential for the","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 May","modification":"2026-06-10T03:14:32.101Z","creation":"2026-06-10T03:08:08.02Z"},"accession":"S-EPMC7199855","cross_references":{"pubmed":["32344433"],"doi":["10.1083/jcb.201811014"]}}