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Cardiolipin: Key Modulator of Potassium Channels
Cardiolipin: Key Modulator of Potassium Channels
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mindyhausler
4 posts
Jul 29, 2025
8:12 PM
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Cardiolipin (CL), a dianionic phospholipid predominantly localized in bacterial and mitochondrial membranes, plays a pivotal role in modulating membrane protein function. In a recent study focused on the potassium channel KcsA from Streptomyces, Cardiolipin was shown to exhibit remarkably high affinity for the channel, particularly under acidic conditions (pH 4.0), mimicking the channel's activated state.
Using a surface plasmon resonance (SPR)-based assay, researchers found that CL binds to both the lipid-sensing N-terminal M0 helix and an additional site within the transmembrane domain, suggesting multiple, functionally relevant interaction points. This contrasts with monoanionic lipids, such as phosphatidic acid (PA), which primarily associate with the M0 helix and show lower affinity. Notably, the dissociation constant (KD) for CL-KcsA interaction at pH 4.0 is in the nanomolar range (KA ? 10?), with a very low off-rate (koff), confirming strong and specific binding under acidic conditions.
Single-channel electrophysiological recordings further revealed that CL significantly enhances KcsA channel opening in an M0-independent manner, supporting a distinct allosteric mechanism of channel modulation.
These findings demonstrate that cardiolipin is used for the modulation of potassium channel activity through high-affinity, pH-dependent interactions, and highlight its essential role in regulating ion channel function in native bacterial membranes.
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