Cancer-specific c-Myc mapping reveals overlooked SLK protein as treatment target
Using a photochemically driven labeling technique, a Cornell-led research group has devised a strategy for capturing cancer-specific protein–protein interactions, which could one day lead to targeted therapies for prostate, small-cell lung, pancreatic and other deadly forms of cancer.
A Cornell-led research team has developed a method to capture cancer-specific protein interactions, potentially paving the way for targeted therapies against prostate, small-cell lung, pancreatic and other deadly cancers. The study, led by assistant professor Ciaran Seath and doctoral student Ryan Milione, focused on the c-Myc protein, which is crucial for tumor growth.
By employing a technique called µMap, the researchers were able to visualize c-Myc's interacting partners inside cancer cells, revealing that a signaling protein called SLK plays a significant role in cancer-specific co-regulation. SLK, which is present at similar concentrations in healthy and cancerous cells, was found to stabilize c-Myc in the nucleus, allowing the transcription factor to function improperly and contribute to cancer growth.
This discovery highlights the importance of protein subcellular localization in cancer and opens up new possibilities for developing therapies that specifically target cancer cells without affecting healthy cells. The researchers are now working on creating therapeutic small molecules based on their findings, with the hope of launching companies and developing clinical treatments.
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