ArticleJournal of molecular biology2013
Structure of a Ca(2+)/CaM:Kv7.4 (KCNQ4) B-helix complex provides insight into M current modulation.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Calmodulation meta-analysis: predicting calmodulin binding via canonical motif clustering.The Journal of general physiology · 2014Pooled it
- HAP1 interaction with KCNQ4 attenuates channel surface expression and function.Molecules and cells · 2026Article
- Isothermal Titration Calorimetry for Fragment-Based Analysis of Ion Channel Interactions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Redox regulation of KeLife · 2023Article
- The Pathological Mechanisms of Hearing Loss Caused byBiomedicines · 2022Review
- Cell death-inducing cytotoxicity in truncated KCNQ4 variants associated with DFNA2 hearing loss.Disease models & mechanisms · 2021Article
- Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021Article
- Pharmacological Activation of Neuronal Voltage-Gated Kv7/KCNQ/M-Channels for Potential Therapy of Epilepsy and Pain.Handbook of experimental pharmacology · 2021Article
- The S2-S3 Loop of Kv7.4 Channels Is Essential for Calmodulin Regulation of Channel Activation.Frontiers in physiology · 2020Article
- Cyclic AMP-Dependent Regulation of Kv7 Voltage-Gated Potassium Channels.Frontiers in physiology · 2020Review
- A mutually induced conformational fit underlies CaThe Journal of biological chemistry · 2019Article
- Reduced axonal surface expression and phosphoinositide sensitivity in KNeurobiology of disease · 2018Article
- Calmodulin: A Multitasking Protein in Kv7.2 Potassium Channel Functions.Biomolecules · 2018Review
- Structural basis and energy landscape for the CaProceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Calmodulin C-Lobe CaNeuron · 2018Article
- Inactivation gating of Kv7.1 channels does not involve concerted cooperative subunit interactions.Channels (Austin, Tex.) · 2018Article
- CaChannels (Austin, Tex.) · 2017Article
- Competition of calcified calmodulin N lobe and PIP2 to an LQT mutation site in Kv7.1 channel.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- FGF14 is a regulator of KCNQ2/3 channels.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mechanisms of Calmodulin Regulation of Different Isoforms of Kv7.4 K+ Channels.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Calmodulin (CaM) is an important regulator of Kv7.x (KCNQx) voltage-gated potassium channels. Channels from this family produce neuronal M currents and cardiac and auditory I(KS) currents and harbor mutations that cause arrhythmias, epilepsy, and deafness. Despite extensive functional characterization, biochemical and structural details of the interaction between CaM and the channel have remained elusive. Here, we show that both apo-CaM and Ca(2+)/CaM bind to the C-terminal tail of the neuronal channel Kv7.4 (KCNQ4), which is involved in both hearing and mechanosensation. Interactions between apo-CaM and the Kv7.4 tail involve two C-terminal tail segments, known as the A and B segments, whereas the interaction between Ca(2+)/CaM and the Kv7.4 C-terminal tail requires only the B segment. Biochemical studies show that the calcium dependence of the CaM:B segment interaction is conserved in all Kv7 subtypes. X-ray crystallographic determination of the structure of the Ca(2+)/CaM:Kv7.4 B segment complex shows that Ca(2+)/CaM wraps around the Kv7.4 B segment, which forms an α-helix, in an antiparallel orientation that embodies a variation of the classic 1-14 Ca(2+)/CaM interaction motif. Taken together with the context of prior studies, our data suggest a model for modulation of neuronal Kv7 channels involving a calcium-dependent conformational switch from an apo-CaM form that bridges the A and B segments to a Ca(2+)/CaM form bound to the B-helix. The structure presented here also provides a context for a number of disease-causing mutations and for further dissection of the mechanisms by which CaM controls Kv7 function.
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