{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["111(18)"],"submitter":["Yuan S"],"pubmed_abstract":["In the past decade, ubiquitination has been well documented to have multifaceted roles in regulating NF-κB activation in mammals. However, its function, especially how deubiquitinating enzymes balance the NF-κB activation, remains largely elusive in invertebrates. Investigating bbtA20 and its binding proteins, bbt A20-binding inhibitor of NF-κB (bbtABIN1) and bbtABIN2, in Chinese amphioxus Branchiostoma belcheri tsingtauense, we found that bbtABIN2 can colocalize and compete with bbt TNF receptor-associated factor 6 to connect the K63-linked polyubiquitin chains, whereas bbtABIN1 physically links bbtA20 to bbt NF-κB essential modulator (bbtNEMO) to facilitate the K48-linked ubiquitination of bbtNEMO. Similar to human A20, bbtA20 is a dual enzyme that removes the K63-linked polyubiquitin ch"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["6720-5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4020044"],"repository":["biostudies-literature"],"pubmed_title":["Emergence of the A20/ABIN-mediated inhibition of NF-κB signaling via modifying the ubiquitinated proteins in a basal chordate."],"pmcid":["PMC4020044"],"pubmed_authors":["Xu L","Yuan S","Ruan J","Dong X","Tao X","Xu A","Peng J"],"additional_accession":[]},"is_claimable":false,"name":"Emergence of the A20/ABIN-mediated inhibition of NF-κB signaling via modifying the ubiquitinated proteins in a basal chordate.","description":"In the past decade, ubiquitination has been well documented to have multifaceted roles in regulating NF-κB activation in mammals. However, its function, especially how deubiquitinating enzymes balance the NF-κB activation, remains largely elusive in invertebrates. Investigating bbtA20 and its binding proteins, bbt A20-binding inhibitor of NF-κB (bbtABIN1) and bbtABIN2, in Chinese amphioxus Branchiostoma belcheri tsingtauense, we found that bbtABIN2 can colocalize and compete with bbt TNF receptor-associated factor 6 to connect the K63-linked polyubiquitin chains, whereas bbtABIN1 physically links bbtA20 to bbt NF-κB essential modulator (bbtNEMO) to facilitate the K48-linked ubiquitination of bbtNEMO. Similar to human A20, bbtA20 is a dual enzyme that removes the K63-linked polyubiquitin ch","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 May","modification":"2026-05-02T19:58:30.252Z","creation":"2026-04-07T18:25:38.084Z"},"accession":"S-EPMC4020044","cross_references":{"pubmed":["24753567"],"doi":["10.1073/pnas.1321187111"]}}