{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T06:51:44Z","timestamp":1792651904520,"version":"4.5.0"},"reference-count":46,"publisher":"American Society of Hematology","issue":"9","content-domain":{"domain":["ashpublications.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2023,3,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Venetoclax combination therapies are becoming the standard of care in acute myeloid leukemia (AML). However, the therapeutic benefit of these drugs in older\/unfit patients is limited to only a few months, highlighting the need for more effective therapies. Protein phosphatase 2A (PP2A) is a tumor suppressor phosphatase with pleiotropic functions that becomes inactivated in \u223c70% of AML cases. PP2A promotes cancer cell death by modulating the phosphorylation state in a variety of proteins along the mitochondrial apoptotic pathway. We therefore hypothesized that pharmacological PP2A reactivation could increase BCL2 dependency in AML cells and, thus, potentiate venetoclax\u2013induced cell death. Here, by using 3 structurally distinct PP2A-activating drugs, we show that PP2A reactivation synergistically enhances venetoclax activity in AML cell lines, primary cells, and xenograft models. Through the use of gene editing tools and pharmacological approaches, we demonstrate that the observed therapeutic synergy relies on PP2A complexes containing the B56\u03b1 regulatory subunit, of which expression dictates response to the combination therapy. Mechanistically, PP2A reactivation enhances venetoclax-driven apoptosis through simultaneous inhibition of antiapoptotic BCL2 and extracellular signal-regulated kinase signaling, with the latter decreasing MCL1 protein stability. Finally, PP2A targeting increases the efficacy of the clinically approved venetoclax and azacitidine combination in\u00a0vitro, in primary cells, and in an AML patient-derived xenograft model. These preclinical results provide a scientific rationale for testing PP2A-activating drugs with venetoclax combinations in AML.<\/jats:p>","DOI":"10.1182\/blood.2022016466","type":"journal-article","created":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T21:07:13Z","timestamp":1669928833000},"page":"1047-1059","update-policy":"https:\/\/doi.org\/10.1182\/blood.2019cm0000","source":"Crossref","is-referenced-by-count":25,"title":["Activation of the PP2A-B56\u03b1 heterocomplex synergizes with venetoclax therapies in AML through BCL2 and MCL1 modulation"],"prefix":"10.1182","volume":"141","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4611-3855","authenticated-orcid":false,"given":"Irene","family":"Peris","sequence":"first","affiliation":[{"name":"1Centro de Investigaci\u00f3n M\u00e9dica Aplicada, University of Navarra, Pamplona, Spain"},{"name":"2Department of Biochemistry and Genetics, University of Navarra, Pamplona, Spain"},{"name":"3Instituto de Investigaci\u00f3n Sanitaria de Navarra, Pamplona, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7020-5819","authenticated-orcid":false,"given":"Silvia","family":"Romero-Murillo","sequence":"additional","affiliation":[{"name":"1Centro de Investigaci\u00f3n M\u00e9dica Aplicada, University of Navarra, Pamplona, Spain"},{"name":"2Department of Biochemistry and Genetics, University of Navarra, Pamplona, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3287-2228","authenticated-orcid":false,"given":"Elena","family":"Mart\u00ednez-Balsalobre","sequence":"additional","affiliation":[{"name":"4Cancer and Aging Group, Hospital Universitario Virgen de la Arrixaca, and Instituto Murciano de Investigaci\u00f3n Biosanitaria, Murcia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1746-1113","authenticated-orcid":false,"given":"Caroline 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