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A Gating Charge Transfer Center in Voltage Sensors

Tao, Xiao and Lee, Alice and Limapichat, Walrati and Dougherty, Dennis A. and MacKinnon, Roderick (2010) A Gating Charge Transfer Center in Voltage Sensors. Science, 328 (5974 ). pp. 67-73. ISSN 0036-8075. PMCID PMC2869078. http://resolver.caltech.edu/CaltechAUTHORS:20100412-093009827

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Abstract

Voltage sensors regulate the conformations of voltage-dependent ion channels and enzymes. Their nearly switchlike response as a function of membrane voltage comes from the movement of positively charged amino acids, arginine or lysine, across the membrane field. We used mutations with natural and unnatural amino acids, electrophysiological recordings, and x-ray crystallography to identify a charge transfer center in voltage sensors that facilitates this movement. This center consists of a rigid cyclic "cap" and two negatively charged amino acids to interact with a positive charge. Specific mutations induce a preference for lysine relative to arginine. By placing lysine at specific locations, the voltage sensor can be stabilized in different conformations, which enables a dissection of voltage sensor movements and their relation to ion channel opening.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1126/science.1185954 DOIArticle
http://www.sciencemag.org/cgi/content/abstract/328/5974/67PublisherArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2869078PubMed CentralArticle
ORCID:
AuthorORCID
Dougherty, Dennis A.0000-0003-1464-2461
Additional Information:© 2010 American Association for the Advancement of Science. Received 14 December 2009; accepted 16 February 2010. We thank members of D. Gadsby’s laboratory (Rockefeller University) for assistance with oocyte preparation; members of the MacKinnon laboratory for assistance; the staff at beamline X29 (National Synchrotron Light Source, Brookhaven National Laboratory) for advice at the synchrotron; and A. Banerjee, J. A. Letts, G. von Heijne (Stockholm University), and J. Chen (Purdue University) for helpful discussions. R.M. is the Investigator in the Howard Hughes Medical Institute. D.A.D. is a George Grant Hoag Professor of Chemistry. Supported by NIH GM43949 to R.M and NS 34407 to D.A.D. The x-ray crystallographic coordinates and structure factor files have been deposited in the Protein Data Bank with accession ID 3LNM.
Funders:
Funding AgencyGrant Number
NIHGM43949
NIHNS34407
PubMed Central ID:PMC2869078
Record Number:CaltechAUTHORS:20100412-093009827
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20100412-093009827
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:17930
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:28 Apr 2010 19:20
Last Modified:14 Nov 2017 21:42

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