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This study shows creatine kinases, including CKMT1A, CKMT1B, and CKB, are highly expressed in cells relying on the mitochondrial F1F0 ATP synthase for survival. Interestingly, silencing CKB, but not CKMT1A or CKMT1B, leads to a loss of sensitivity to the inhibition of F1F0 ATP synthase in these cells. Mechanistically, CKB promotes mitochondrial ATP but reduces glycolytic ATP production by suppressing mitochondrial calcium (mCa\n                    <jats:sup>2+<\/jats:sup>\n                    ) levels, thereby preventing the activation of mitochondrial permeability transition pore (mPTP) and ensuring efficient mitochondrial ATP generation. Further, CKB achieves this regulation by suppressing mCa\n                    <jats:sup>2+<\/jats:sup>\n                    levels through the inhibition of AKT activity. Notably, the CKB\u2010AKT signaling axis boosts mitochondrial ATP production in cancer cells growing in a mouse tumor model. Moreover, this study also uncovers a decline in CKB expression in peripheral blood mononuclear cells with aging, accompanied by an increase in AKT signaling in these cells. These findings thus shed light on a novel signaling pathway involving CKB that directly regulates mitochondrial ATP production, potentially playing a role in both pathological and physiological conditions.\n                  <\/jats:p>","DOI":"10.1002\/advs.202403093","type":"journal-article","created":{"date-parts":[[2024,6,19]],"date-time":"2024-06-19T15:20:11Z","timestamp":1718810411000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["CKB Promotes Mitochondrial ATP Production by Suppressing Permeability Transition Pore"],"prefix":"10.1002","volume":"11","author":[{"given":"Le","family":"He","sequence":"first","affiliation":[{"name":"Tongji University Cancer Center Shanghai Tenth People's Hospital of Tongji University School of Medicine Tongji University  Shanghai 200092 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