ArticleACS chemical biology2018
Protein-Lipid Interfaces Can Drive the Functions of Membrane-Embedded Protein-Protein Complexes.
Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Genome-Wide Identification of theInternational journal of molecular sciences · 2026Article
- Colorimetric and Fluorometric N-Acylhydrazone-based Chemosensors for Detection of Single to Multiple Metal Ions: Design Strategies and Analytical Applications.Journal of fluorescence · 2025Review
- Dissecting the contributions of membrane affinity and bivalency of the spider venom protein DkTx to its sustained mode of TRPV1 activation.The Journal of biological chemistry · 2023Article
- Venom Peptide Toxins Targeting the Outer Pore Region of Transient Receptor Potential Vanilloid 1 in Pain: Implications for Analgesic Drug Development.International journal of molecular sciences · 2022Review
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- Distinct classes of multi-subunit heterogeneity: analysis using Fourier Transform methods and native mass spectrometry.The Analyst · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The roles of surrounding membrane lipids in the functions of transmembrane and peripheral membrane proteins are largely unknown. Herein, we utilize the recently reported structures of the TRPV1 ion channel protein bound to its potent protein agonist, the double-knot toxin (DkTx), as a model system to investigate the roles of toxin-lipid interfaces in TRPV1 activation by characterizing a series of DkTx variants electrophysiologically. Together with membrane partitioning experiments, these studies reveal that toxin-lipid interfaces play an overwhelmingly dominant role in channel activation as compared to lipid-devoid toxin-channel interfaces. Additionally, we find that whereas the membrane interfaces formed by one of the knots of the toxin endow it with its low channel-dissociation rate, those formed by other knot contribute primarily to its potency. These studies establish that protein-lipid interfaces play nuanced yet profound roles in the function of protein-protein complexes within membranes.
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Registered trials
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