ArticleExperimental and therapeutic medicine2026
Interacting proteins of AMPK studied using TurboID proximity labeling technology.
Article in Experimental and therapeutic medicine, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
In living organisms, the change in the adenosine 5'-monophosphate (AMP)/adenosine 5'-triphosphate ratio serves as a key signal regulating AMP-activated protein kinase (AMPK) activity, which is an important molecule for the control of cellular energy metabolism and serves a key role in a number of diseases, such as diabetes and myocardial infarction. To explore novel AMPK-interacting proteins and investigate their biological functions, the present study used TurboID proximity labeling in U251 cells stably expressing AMPK-TurboID. Novel AMPK-interacting proteins were explored under both normal and CCCP-treated conditions to investigate their biological functions. Stable cell lines overexpressing AMPK-TurboID were successfully established, and interacting proteins were identified through biotin labeling, silver staining and mass spectrometry analysis. Due to the involvement of AMPK in numerous metabolic pathways and the advantages of TurboID over traditional techniques, including its high temporal resolution,
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