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Dynamic protein-protein interactions of KCNQ1 and KCNE1 measured by EPR line shape analysis.
- Source :
-
Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2024 Oct; Vol. 1866 (7), pp. 184377. Date of Electronic Publication: 2024 Aug 03. - Publication Year :
- 2024
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Abstract
- KCNQ1, also known as Kv7.1, is a voltage gated potassium channel that associates with the KCNE protein family. Mutations in this protein has been found to cause a variety of diseases including Long QT syndrome, a type of cardiac arrhythmia where the QT interval observed on an electrocardiogram is longer than normal. This condition is often aggravated during strenuous exercise and can cause fainting spells or sudden death. KCNE1 is an ancillary protein that interacts with KCNQ1 in the membrane at varying molar ratios. This interaction allows for the flow of potassium ions to be modulated to facilitate repolarization of the heart. The interaction between these two proteins has been studied previously with cysteine crosslinking and electrophysiology. In this study, electron paramagnetic resonance (EPR) spectroscopy line shape analysis in tandem with site directed spin labeling (SDSL) was used to observe changes in side chain dynamics as KCNE1 interacts with KCNQ1. KCNE1 was labeled at different sites that were found to interact with KCNQ1 based on previous literature, along with sites outside of that range as a control. Once labeled KCNE1 was incorporated into vesicles, KCNQ1 (helices S1-S6) was titrated into the vesicles. The line shape differences observed upon addition of KCNQ1 are indicative of an interaction between the two proteins. This method provides a first look at the interactions between KCNE1 and KCNQ1 from a dynamics perspective using the full transmembrane portion of KCNQ1.<br />Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2024 Elsevier B.V. All rights reserved.)
- Subjects :
- Electron Spin Resonance Spectroscopy methods
Protein Binding
Humans
Animals
Long QT Syndrome metabolism
Long QT Syndrome genetics
Potassium Channels, Voltage-Gated metabolism
Potassium Channels, Voltage-Gated genetics
Potassium Channels, Voltage-Gated chemistry
KCNQ1 Potassium Channel metabolism
KCNQ1 Potassium Channel genetics
KCNQ1 Potassium Channel chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1879-2642
- Volume :
- 1866
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta. Biomembranes
- Publication Type :
- Academic Journal
- Accession number :
- 39103068
- Full Text :
- https://doi.org/10.1016/j.bbamem.2024.184377