{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T09:00:52Z","timestamp":1781168452166,"version":"3.54.1"},"reference-count":29,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2025,4,14]],"date-time":"2025-04-14T00:00:00Z","timestamp":1744588800000},"content-version":"vor","delay-in-days":13,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2025,4,1]],"date-time":"2025-04-01T00:00:00Z","timestamp":1743465600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J Biochem &amp;amp; Molecular Tox"],"published-print":{"date-parts":[[2025,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>Lysine succinyltransferase KAT3B plays a critical role in the progression of various cancers by modulating key metabolic pathways, including glycolysis. However, the function and underlying mechanism of KAT3B in glycolysis and lung cancer (LC) progression remain to be further studied. We determined mRNA expression levels of lysine succinyl\u2010modifying enzymes through qRT\u2010PCR. Protein expression and succinylation status of glycolysis\u2010related proteins PKM2, LDHA, and ENO1 were analyzed via Western blot. Co\u2010immunoprecipitation and immunofluorescence microscopy were employed to verify the interaction between KAT3B and PKM2. Bioinformatics analysis predicted succinylation sites on PKM2, which were subsequently validated through site\u2010directed mutagenesis. The effects of KAT3B and PKM2 on LC cell malignancy and glycolysis were evaluated using CCK\u20108, transwell migration, glucose uptake, lactate production, ECAR, and OCR assays. A xenograft tumor model was utilized to assess the impact of KAT3B on LC tumor growth. We confirmed the augmentation of KAT3B in LC, which also was correlated with advanced TNM stages and elevated T stages of LC patients. Conversely, KAT3B knockdown suppressed the growth, metastasis, and glycolytic activity of LC cells in vitro, while also inhibiting tumor growth in vivo. KAT3B mediated succinylation at PKM2 K298, and the suppression of LC cell malignancy and glycolysis upon KAT3B downregulation was largely reversed by upregulation of PKM2. The KAT3B\/PKM2 axis may be a novel target for LC therapy.<\/jats:p>","DOI":"10.1002\/jbt.70259","type":"journal-article","created":{"date-parts":[[2025,4,14]],"date-time":"2025-04-14T08:40:51Z","timestamp":1744620051000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["KAT3B Promotes the Glycolysis and Malignant Progression of Lung Cancer by Mediating the Succinylation Modification of PKM2"],"prefix":"10.1002","volume":"39","author":[{"given":"Zhifeng","family":"Guo","sequence":"first","affiliation":[{"name":"Department of Oncology, Section II Chifeng Municipal Hospital, Chifeng 024000, Inner Mongolia Autonomous Region  China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan","family":"Hui","sequence":"additional","affiliation":[{"name":"Department of Oncology, Section II Chifeng Municipal Hospital, Chifeng 024000, Inner Mongolia Autonomous Region  China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Siqi","family":"Sun","sequence":"additional","affiliation":[{"name":"Department of Oncology, Section II Chifeng Municipal Hospital, Chifeng 024000, Inner Mongolia Autonomous Region  China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-6661-4373","authenticated-orcid":false,"given":"Fanlong","family":"Kong","sequence":"additional","affiliation":[{"name":"Department of Oncology, Section II Chifeng Municipal Hospital, Chifeng 024000, Inner Mongolia Autonomous Region  China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2025,4,14]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.1080\/21655979.2021.1886771"},{"key":"e_1_2_11_3_1","doi-asserted-by":"publisher","DOI":"10.3322\/caac.21660"},{"key":"e_1_2_11_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(16)30958-8"},{"key":"e_1_2_11_5_1","doi-asserted-by":"publisher","DOI":"10.3389\/fonc.2022.1081712"},{"key":"e_1_2_11_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2023.115713"},{"key":"e_1_2_11_7_1","doi-asserted-by":"publisher","DOI":"10.1089\/ars.2017.7264"},{"issue":"10","key":"e_1_2_11_8_1","first-page":"4683","article-title":"Role of Succinylation Modification in Thyroid Cancer and Breast Cancer","volume":"11","author":"Mu R.","year":"2021","journal-title":"American Journal of Cancer Research"},{"key":"e_1_2_11_9_1","doi-asserted-by":"publisher","DOI":"10.1111\/jcmm.13920"},{"key":"e_1_2_11_10_1","doi-asserted-by":"crossref","unstructured":"X. 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