<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kaneko Y</submitter><funding>Ministry of Education, Culture, Sports, Science and Technology</funding><pagination>e105853</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8090856</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>40(9)</volume><pubmed_abstract>p97ATPase-mediated membrane fusion is required for the biogenesis of the Golgi complex. p97 and its cofactor p47 function in soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE) priming, but the tethering complex for p97/p47-mediated membrane fusion remains unknown. In this study, we identified formiminotransferase cyclodeaminase (FTCD) as a novel p47-binding protein. FTCD mainly localizes to the Golgi complex and binds to either p47 or p97 via its association with their polyglutamate motifs. FTCD functions in p97/p47-mediated Golgi reassembly at mitosis in vivo and in vitro via its binding to p47 and to p97. We also showed that FTCD, p47, and p97 form a big FTCD-p97/p47-FTCD tethering complex. In vivo tethering assay revealed that FTCD that was designed to l</pubmed_abstract><journal>The EMBO journal</journal><pubmed_title>p97 and p47 function in membrane tethering in cooperation with FTCD during mitotic Golgi reassembly.</pubmed_title><pmcid>PMC8090856</pmcid><funding_grant_id>16K07353</funding_grant_id><pubmed_authors>Kaneko Y</pubmed_authors><pubmed_authors>Goto Y</pubmed_authors><pubmed_authors>Zhang X</pubmed_authors><pubmed_authors>Kondo H</pubmed_authors><pubmed_authors>Ayala R</pubmed_authors><pubmed_authors>Shimoda K</pubmed_authors><pubmed_authors>Panico S</pubmed_authors></additional><is_claimable>false</is_claimable><name>p97 and p47 function in membrane tethering in cooperation with FTCD during mitotic Golgi reassembly.</name><description>p97ATPase-mediated membrane fusion is required for the biogenesis of the Golgi complex. p97 and its cofactor p47 function in soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE) priming, but the tethering complex for p97/p47-mediated membrane fusion remains unknown. In this study, we identified formiminotransferase cyclodeaminase (FTCD) as a novel p47-binding protein. FTCD mainly localizes to the Golgi complex and binds to either p47 or p97 via its association with their polyglutamate motifs. FTCD functions in p97/p47-mediated Golgi reassembly at mitosis in vivo and in vitro via its binding to p47 and to p97. We also showed that FTCD, p47, and p97 form a big FTCD-p97/p47-FTCD tethering complex. In vivo tethering assay revealed that FTCD that was designed to l</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 May</publication><modification>2026-06-01T03:08:40.508Z</modification><creation>2025-04-05T19:57:24.673Z</creation></dates><accession>S-EPMC8090856</accession><cross_references><pubmed>33555040</pubmed><doi>10.15252/embj.2020105853</doi></cross_references></HashMap>