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Updated: Feb 6, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Remote-Controlling Potassium Channels in Living Cells through Photothermal Inactivation of Calmodulin
Ran Chai1,2, Chengfen Xing1,2, Dong Gao2
1School of Materials Science and Engineering, Hebei University of Technology, Tianjin, 300130, P. R. China.
Abstract:
Spatiotemporal regulation of cellular functions provides a powerful strategy for understanding underlying mechanisms of cellular bioprocesses. Here, a strategy is reported to realize the remote control of the activities of potassium channels via photothermal inactivation of calmodulin (CaM) by using reduced graphene oxide decorated with calmodulin binding peptide (rGO-P) as the transducer with near-infrared light (NIR) irradiation. Upon NIR light irradiation, the CaM/Ca2+ bound to rGO-P is inactivated by the photothermal effect of rGO-P, resulting in the incapability of binding with Ca2+ . Hence, the closed Kv10.1 channel is converted to be open in the presence of calcium in living cells. Meanwhile, the SK2 channel is induced to be closed from the open state and the Kir2.1 channel is unaffected by the intracellular inactivation of CaM. This strategy gives a noninvasive and effective approach to remotely control the activities of potassium channels, offering an alternative for the development of optogenetics.
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