Scientists have unveiled the structure of uMtCK, a key enzyme cancer cells use for energy, offering new insights for targeted therapies to slow tumor growth.
Cancer cells are notorious for their insatiable hunger for energy, rapidly multiplying and hijacking normal cellular functions to meet their fuel demands. One of the critical processes they exploit involves a group of enzymes called creatine kinases (CK), which are responsible for shuttling energy within cells. A specific type of CK, known as ubiquitous mitochondrial creatine kinase (uMtCK), plays a crucial role in helping cancer cells tap into and distribute energy, making it an essential target for potential cancer therapies.
In a breakthrough study, scientists from Sanford Burnham Prebys and Mayo Clinic revealed the detailed structure of human uMtCK, uncovering how its shape changes when bound to energy molecules like creatine or adenosine triphosphate (ATP). Using cutting-edge cryogenic electron microscopy (cryo-EM), the team created 3D images of the protein and its interactions, offering insights that could pave the way for developing drugs to block this crucial energy transport mechanism in cancer cells.
Their research, published in Structure on February 3, 2025, also tested an existing CK inhibitor called CKi on breast cancer cells. The results showed that CKi was effective in slowing down breast cancer cell growth, confirming the potential of targeting this pathway in cancer treatment. However, the inhibitor isn’t selective for uMtCK alone, and could disrupt other vital processes, leading to high toxicity.
Building on these findings, the researchers are now working to design more targeted inhibitors that specifically block uMtCK without affecting other cellular functions, offering the promise of more effective and less toxic cancer therapies in the future.
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