{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe provided abstracts do not describe any function for KCNAB1‐AS2. Instead, they focus on the activities of UBE2L3 in key cellular processes. In the first study, UBE2L3 is shown to be an indirect target of caspase‐1 during inflammasome activation, where it is proteasomally degraded in a manner independent of both pyroptosis and ubiquitin signaling. This degradation reduces UBE2L3’s post‐translational promotion of K48‐ubiquitylation and turnover of pro–IL-1β, thereby limiting the production of mature IL-1β and restraining the inflammatory response."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn a second study, UBE2L3 is described in the context of skeletal muscle atrophy. Here, UBE2L3 interacts with the E3 ligase MuRF1 to regulate the degradation of contractile proteins such as alpha–actin and myosin heavy chain (MHC). The modulation of these proteins by UBE2L3 affects muscle mass, where its knockdown leads to hypertrophy and overexpression exacerbates muscle wasting under catabolic conditions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA third study further substantiates the role of UBE2L3 in inflammatory regulation by showing that its deletion in mice results in an accumulation of pro–IL-1β, ultimately driving excessive mature IL-1β production and subsequent inflammatory damage. The work identifies E3 ligases TRIP12 and AREL1 as partners in the process, which add destabilizing poly-ubiquitin chains to pro–IL-1β, emphasizing the importance of precursor abundance in controlling cytokine output."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nWhile these studies provide detailed insights into the regulation of inflammation and muscle atrophy by UBE2L3 and its associated pathways, none of them address or mention KCNAB1‐AS2. Therefore, the function of KCNAB1‐AS2 remains undefined in the context of these abstracts and would require separate investigation to elucidate any potential roles it might have in these or related biological processes.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Matthew J G Eldridge, Julia Sanchez-Garrido, Gil Ferreira Hoben, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Atypical Ubiquitin E2 Conjugase UBE2L3 Is an Indirect Caspase-1 Target and Controls IL-1β Secretion by Inflammasomes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Rep (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.celrep.2017.01.015"}], "href": "https://doi.org/10.1016/j.celrep.2017.01.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28147281"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28147281"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Dulce Peris-Moreno, Mélodie Malige, Agnès Claustre, et al. "}, {"type": "b", "children": [{"type": "t", "text": "UBE2L3, a Partner of MuRF1/TRIM63, Is Involved in the Degradation of Myofibrillar Actin and Myosin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cells (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/cells10081974"}], "href": "https://doi.org/10.3390/cells10081974"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34440743"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34440743"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Vishwas Mishra, Anna Crespo-Puig, Callum McCarthy, et al. "}, {"type": "b", "children": [{"type": "t", "text": "IL-1β turnover by the UBE2L3 ubiquitin conjugating enzyme and HECT E3 ligases limits inflammation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-023-40054-x"}], "href": "https://doi.org/10.1038/s41467-023-40054-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37474493"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37474493"}]}]}]}