{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang Y"],"funding":["National Key R&D Program of China","National Natural Science Foundation","National Key R&D Program of China","Natural Science Foundation of Shanghai","Youth Eastern Scholar of Shanghai","National Natural Science Foundation of China","Pujiang talent Program in Shanghai"],"pagination":["8282"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9368767"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(15)"],"pubmed_abstract":["Sirtuin 3 (SIRT3) deacetylase is a key regulator for chemoresistance in acute myeloid leukemia (AML) cells due to its capability of modulating mitochondrial metabolism and reactive oxygen species (ROS). SIRT3 is de-SUMOylated by SUMO-specific peptidase 1 (SENP1), which enhances its deacetylase activity. Therefore, dysregulation of SIRT3 SUMOylation may lead to fortified chemoresistance in AML. Indeed, SIRT3 de-SUMOylation was induced by chemotherapeutic agents, which in turn, exacerbated resistance against chemotherapies in AML by activating SIRT3 via preventing its proteasome degradation. Furthermore, RNA-seq revealed that expression of a collection of genes was altered by SIRT3 de-SUMOylation including inhibition of transcription factor Hes Family BHLH Transcription Factor 1 (HES1), a do"],"journal":["International journal of molecular sciences"],"pubmed_title":["Dysregulation of SIRT3 SUMOylation Confers AML Chemoresistance via Controlling HES1-Dependent Fatty Acid Oxidation."],"pmcid":["PMC9368767"],"funding_grant_id":["17ZR1415600","1730000034","17PJ1405500","81700134","2020YFA0803603"],"pubmed_authors":["Zhang Y","Ren Y","Wang W","Ma J","Wei W","Jiang D","Shen Y","Fan Q","Peng Z","Cheng J"],"additional_accession":[]},"is_claimable":false,"name":"Dysregulation of SIRT3 SUMOylation Confers AML Chemoresistance via Controlling HES1-Dependent Fatty Acid Oxidation.","description":"Sirtuin 3 (SIRT3) deacetylase is a key regulator for chemoresistance in acute myeloid leukemia (AML) cells due to its capability of modulating mitochondrial metabolism and reactive oxygen species (ROS). SIRT3 is de-SUMOylated by SUMO-specific peptidase 1 (SENP1), which enhances its deacetylase activity. Therefore, dysregulation of SIRT3 SUMOylation may lead to fortified chemoresistance in AML. Indeed, SIRT3 de-SUMOylation was induced by chemotherapeutic agents, which in turn, exacerbated resistance against chemotherapies in AML by activating SIRT3 via preventing its proteasome degradation. Furthermore, RNA-seq revealed that expression of a collection of genes was altered by SIRT3 de-SUMOylation including inhibition of transcription factor Hes Family BHLH Transcription Factor 1 (HES1), a do","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jul","modification":"2026-06-22T03:18:04.667Z","creation":"2025-02-19T03:32:04.468Z"},"accession":"S-EPMC9368767","cross_references":{"pubmed":["35955415"],"doi":["10.3390/ijms23158282"]}}