{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang W"],"funding":["Deutsche Forschungsgemeinschaft","Heinz Götze Memorial Fellowship"],"pagination":["877-894"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5839787"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["217(3)"],"pubmed_abstract":["The paralogous Brr6 and Brl1 are conserved integral membrane proteins of the nuclear envelope (NE) with an unclear role in nuclear pore complex (NPC) biogenesis. Here, we analyzed double-degron mutants of Brr6/Brl1 to understand this function. Depletion of Brr6 and Brl1 caused defects in NPC biogenesis, whereas the already assembled NPCs remained unaffected. This NPC biogenesis defect was not accompanied by a change in lipid composition. However, Brl1 interacted with Ndc1 and Nup188 by immunoprecipitation, and with transmembrane and outer and inner ring NPC components by split yellow fluorescent protein analysis, indicating a direct role in NPC biogenesis. Consistently, we found that Brr6 and Brl1 associated with a subpopulation of NPCs and emerging NPC assembly sites. Moreover, <i>BRL1</i"],"journal":["The Journal of cell biology"],"pubmed_title":["Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis."],"pmcid":["PMC5839787"],"funding_grant_id":["SFB/TRR83","Schi 295/5-2"],"pubmed_authors":["Zhang W","Luchtenborg C","Brugger B","Ruthnick D","Sachsenheimer T","Schiebel E","Neuner A"],"additional_accession":[]},"is_claimable":false,"name":"Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis.","description":"The paralogous Brr6 and Brl1 are conserved integral membrane proteins of the nuclear envelope (NE) with an unclear role in nuclear pore complex (NPC) biogenesis. Here, we analyzed double-degron mutants of Brr6/Brl1 to understand this function. Depletion of Brr6 and Brl1 caused defects in NPC biogenesis, whereas the already assembled NPCs remained unaffected. This NPC biogenesis defect was not accompanied by a change in lipid composition. However, Brl1 interacted with Ndc1 and Nup188 by immunoprecipitation, and with transmembrane and outer and inner ring NPC components by split yellow fluorescent protein analysis, indicating a direct role in NPC biogenesis. Consistently, we found that Brr6 and Brl1 associated with a subpopulation of NPCs and emerging NPC assembly sites. Moreover, <i>BRL1</i","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Mar","modification":"2026-05-06T03:45:36.61Z","creation":"2019-10-30T08:13:39Z"},"accession":"S-EPMC5839787","cross_references":{"pubmed":["29439116"],"doi":["10.1083/jcb.201706024"]}}