<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Lucken-Ardjomande Hasler S</submitter><funding>Swiss National Science Foundation</funding><funding>Medical Research Council</funding><pagination>e201811014</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7199855</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>219(5)</volume><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</pubmed_abstract><journal>The Journal of cell biology</journal><pubmed_title>GRAF2, WDR44, and MICAL1 mediate Rab8/10/11-dependent export of E-cadherin, MMP14, and CFTR ΔF508.</pubmed_title><pmcid>PMC7199855</pmcid><funding_grant_id>PA00P3-124164</funding_grant_id><funding_grant_id>PBGE1-121206</funding_grant_id><funding_grant_id>MC_U105178795</funding_grant_id><funding_grant_id>U105178795</funding_grant_id><pubmed_authors>Pasche M</pubmed_authors><pubmed_authors>Lucken-Ardjomande Hasler S</pubmed_authors><pubmed_authors>McMahon HT</pubmed_authors><pubmed_authors>Vallis Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>GRAF2, WDR44, and MICAL1 mediate Rab8/10/11-dependent export of E-cadherin, MMP14, and CFTR ΔF508.</name><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</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 May</publication><modification>2026-06-10T03:14:32.101Z</modification><creation>2026-06-10T03:08:08.02Z</creation></dates><accession>S-EPMC7199855</accession><cross_references><pubmed>32344433</pubmed><doi>10.1083/jcb.201811014</doi></cross_references></HashMap>