{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ryan KJ"],"funding":["NIGMS NIH HHS"],"pagination":["886-98"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1805111"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(3)"],"pubmed_abstract":["Nuclear pore complex (NPC) assembly in interphase cells requires that new NPCs insert into an intact nuclear envelope (NE). Our previous work identified the Ran GTPase as an essential component in this process. We proposed that Ran is required for targeting assembly factors to the cytoplasmic NE face via a novel, vesicular intermediate. Although the molecular target was not identified, Ran is known to function by modulating protein interactions for karyopherin (Kap) beta family members. Here we characterize loss-of-function Saccharomyces cerevisiae mutants in KAP95 with blocks in NPC assembly. Similar to defects in Ran cycle mutants, nuclear pore proteins are no longer localized properly to the NE in kap95 mutants. Also like Ran cycle mutants, the kap95-E126K mutant displayed enhanced leth"],"journal":["Molecular biology of the cell"],"pubmed_title":["The karyopherin Kap95 regulates nuclear pore complex assembly into intact nuclear envelopes in vivo."],"pmcid":["PMC1805111"],"funding_grant_id":["R01 GM-57438","R01 GM057438"],"pubmed_authors":["Ryan KJ","Zhou Y","Wente SR"],"additional_accession":[]},"is_claimable":false,"name":"The karyopherin Kap95 regulates nuclear pore complex assembly into intact nuclear envelopes in vivo.","description":"Nuclear pore complex (NPC) assembly in interphase cells requires that new NPCs insert into an intact nuclear envelope (NE). Our previous work identified the Ran GTPase as an essential component in this process. We proposed that Ran is required for targeting assembly factors to the cytoplasmic NE face via a novel, vesicular intermediate. Although the molecular target was not identified, Ran is known to function by modulating protein interactions for karyopherin (Kap) beta family members. Here we characterize loss-of-function Saccharomyces cerevisiae mutants in KAP95 with blocks in NPC assembly. Similar to defects in Ran cycle mutants, nuclear pore proteins are no longer localized properly to the NE in kap95 mutants. Also like Ran cycle mutants, the kap95-E126K mutant displayed enhanced leth","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Mar","modification":"2025-04-07T12:57:12.174Z","creation":"2019-03-27T02:03:28Z"},"accession":"S-EPMC1805111","cross_references":{"pubmed":["17182855"],"doi":["10.1091/mbc.e06-06-0525"]}}