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Determining the molecular basis of voltage sensitivity in membrane proteins
KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Engineering Sciences (SCI), Applied Physics.
KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Engineering Sciences (SCI), Applied Physics.ORCID iD: 0000-0002-2734-2794
KTH, School of Engineering Sciences (SCI), Applied Physics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
2018 (English)In: The Journal of General Physiology, ISSN 0022-1295, E-ISSN 1540-7748, Vol. 215, no 10, p. 1444-1458Article in journal (Refereed) Published
Abstract [en]

Voltage-sensitive membrane proteins are united by their ability to transform changes in membrane potential into mechanical work. They are responsible for a spectrum of physiological processes in living organisms, including electrical signaling and cell-cycle progression. Although the mechanism of voltage-sensing has been well characterized for some membrane proteins, including voltage-gated ion channels, even the location of the voltage-sensing elements remains unknown for others. Moreover, the detection of these elements by using experimental techniques is challenging because of the diversity of membrane proteins. Here, we provide a computational approach to predict voltage-sensing elements in any membrane protein, independent of its structure or function. It relies on an estimation of the propensity of a protein to respond to changes in membrane potential. We first show that this property correlates well with voltage sensitivity by applying our approach to a set of voltage-sensitive and voltage-insensitive membrane proteins. We further show that it correctly identifies authentic voltage-sensitive residues in the voltage-sensor domain of voltage-gated ion channels. Finally, we investigate six membrane proteins for which the voltage-sensing elements have not yet been characterized and identify residues and ions that might be involved in the response to voltage. The suggested approach is fast and simple and enables a characterization of voltage sensitivity that goes beyond mere identification of charges. We anticipate that its application before mutagenesis experiments will significantly reduce the number of potential voltage-sensitive elements to be tested. 

Place, publisher, year, edition, pages
Rockefeller University Press , 2018. Vol. 215, no 10, p. 1444-1458
National Category
Physical Sciences
Identifiers
URN: urn:nbn:se:kth:diva-236661DOI: 10.1085/jgp.201812086ISI: 000447673900012Scopus ID: 2-s2.0-85054072236OAI: oai:DiVA.org:kth-236661DiVA, id: diva2:1262801
Funder
Swedish Research Council, 2017-04641Science for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

Export Date: 22 October 2018; Article; CODEN: JGPLA; Correspondence Address: Delemotte, L.; Department of Applied Physics, Science for Life Laboratory, KTH Royal Institute of TechnologySweden; email: lucie.delemotte@scilifelab.se. QC 20181113

Available from: 2018-11-13 Created: 2018-11-13 Last updated: 2018-11-13Bibliographically approved

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Kasimova, Marina A.Lindahl, Erik

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