ArticleThe Journal of general physiology1998
Structural implications of fluorescence quenching in the Shaker K+ channel.
Article in The Journal of general physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.
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Who cites it
93 citing papers in PubMed, 141 citations in OpenAlex.
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- Electrically silent mutants unravel the mechanism of binding-gating coupling in Cys-loop receptors.Science advances · 2024Article
- Voltage-clamp fluorometry for advancing mechanistic understanding of ion channel mechanisms with a focus on acid-sensing ion channels.Biochemical Society transactions · 2024Review
- Different fluorescent labels report distinct components of spHCN channel voltage sensor movement.The Journal of general physiology · 2024Article
- Fifty years of gating currents and channel gating.The Journal of general physiology · 2023Review
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- The 70-year search for the voltage-sensing mechanism of ion channels.The Journal of physiology · 2022Article
- The contribution of voltage clamp fluorometry to the understanding of channel and transporter mechanisms.The Journal of general physiology · 2019Review
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- Methodological improvements for fluorescence recordings inThe Journal of general physiology · 2019Article
- The molecular mechanism of SLC34 proteins: insights from two decades of transport assays and structure-function studies.Pflugers Archiv : European journal of physiology · 2019Review
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Gating modulation of the KCNQ1 channel by KCNE proteins studied by voltage-clamp fluorometry.Biophysics and physicobiology · 2019Review
- Permeating disciplines: Overcoming barriers between molecular simulations and classical structure-function approaches in biological ion transport.Biochimica et biophysica acta. Biomembranes · 2018Review
- Active site voltage clamp fluorometry of the sodium glucose cotransporter hSGLT1.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mechanism of functional interaction between potassium channel Kv1.3 and sodium channel NavBeta1 subunit.Scientific reports · 2017Article
- Cation Interactions and Membrane Potential Induce Conformational Changes in NaPi-IIb.Biophysical journal · 2016Article
- Voltage Clamp Fluorometry of P-Type ATPases.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Single-molecule fluorimetry and gating currents inspire an improved optical voltage indicator.eLife · 2015Article
- NS1643 interacts around L529 of hERG to alter voltage sensor movement on the path to activation.Biophysical journal · 2015Article
33 more citing papers are in PubMed but not listed here.
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2 authors at 1 institution in 1 country.
Funding
Abstract
When attached to specific sites near the S4 segment of the nonconducting (W434F) Shaker potassium channel, the fluorescent probe tetramethylrhodamine maleimide undergoes voltage-dependent changes in intensity that correlate with the movement of the voltage sensor (Mannuzzu, L.M., M.M. Moronne, and E.Y. Isacoff. 1996. Science. 271:213-216; Cha, A., and F. Bezanilla. 1997. Neuron. 19:1127-1140). The characteristics of this voltage-dependent fluorescence quenching are different in a conducting version of the channel with a different pore substitution (T449Y). Blocking the pore of the T449Y construct with either tetraethylammonium or agitoxin removes a fluorescence component that correlates with the voltage dependence but not the kinetics of ionic activation. This pore-mediated modulation of the fluorescence quenching near the S4 segment suggests that the fluorophore is affected by the state of the external pore. In addition, this modulation may reflect conformational changes associated with channel opening that are prevented by tetraethylammonium or agitoxin. Studies of pH titration, collisional quenchers, and anisotropy indicate that fluorophores attached to residues near the S4 segment are constrained by a nearby region of protein. The mechanism of fluorescence quenching near the S4 segment does not involve either reorientation of the fluorophore or a voltage-dependent excitation shift and is different from the quenching mechanism observed at a site near the S2 segment. Taken together, these results suggest that the extracellular portion of the S4 segment resides in an aqueous protein vestibule and is influenced by the state of the external pore.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.