{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wackernagel LM"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["6778"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9223704"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(12)"],"pubmed_abstract":["The NF-κB pathway is central pathway for inflammatory and immune responses, and IKKγ/NEMO is essential for NF-κB activation. In a previous report, we identified the role of glycogen synthase kinase-3β (GSK-3β) in NF-κB activation by regulating IKKγ/NEMO. Here, we show that NEMO phosphorylation by GSK-3β leads to NEMO localization into multivesicular bodies (MVBs). Using the endosome marker Rab5, we observed localization into endosomes. Using siRNA, we identified the AAA-ATPase Vps4A, which is involved in recycling the ESCRT machinery by facilitating its dissociation from endosomal membranes, which is necessary for NEMO stability and NF-κB activation. Co-immunoprecipitation studies of NEMO and mutated NEMO demonstrated its direct interaction with Vps4A, which requires NEMO phosphorylation. "],"journal":["International journal of molecular sciences"],"pubmed_title":["IKKγ/NEMO Localization into Multivesicular Bodies."],"pmcid":["PMC9223704"],"funding_grant_id":["97850925-SFB854","361210922/GRK2408"],"pubmed_authors":["Medunjanin S","Fischer KD","Wackernagel LM","Weinert S","Zuschratter W","Richter K","Braun-Dullaeus RC","Abdi Sarabi M"],"additional_accession":[]},"is_claimable":false,"name":"IKKγ/NEMO Localization into Multivesicular Bodies.","description":"The NF-κB pathway is central pathway for inflammatory and immune responses, and IKKγ/NEMO is essential for NF-κB activation. In a previous report, we identified the role of glycogen synthase kinase-3β (GSK-3β) in NF-κB activation by regulating IKKγ/NEMO. Here, we show that NEMO phosphorylation by GSK-3β leads to NEMO localization into multivesicular bodies (MVBs). Using the endosome marker Rab5, we observed localization into endosomes. Using siRNA, we identified the AAA-ATPase Vps4A, which is involved in recycling the ESCRT machinery by facilitating its dissociation from endosomal membranes, which is necessary for NEMO stability and NF-κB activation. Co-immunoprecipitation studies of NEMO and mutated NEMO demonstrated its direct interaction with Vps4A, which requires NEMO phosphorylation. ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2025-04-26T15:34:06.538Z","creation":"2025-02-19T03:51:38.833Z"},"accession":"S-EPMC9223704","cross_references":{"pubmed":["35743220"],"doi":["10.3390/ijms23126778"]}}