NDLI: Crystal Structure and Molecular Imaging of the $Na_{v}$ Channel β3 Subunit Indicates a Trimeric $Assembly^{*}$

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Crystal Structure and Molecular Imaging of the $Na_{v}$ Channel β3 Subunit Indicates a Trimeric $Assembly^{*}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Klingauf, Jurgen Namadurai, Sivakumar Wiemhöfer, Martin Chirgadze, Dimitri Y. Balasuriya, Dilshan Edwardson, J. Michael Jackson, Antony P. Stott, Katherine Rajappa, Rajit
Description	Author Affiliation: Namadurai S ( From the Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, United Kingdom.)
Abstract	The vertebrate sodium $(Na_{v})$ channel is composed of an ion-conducting α subunit and associated β subunits. Here, we report the crystal structure of the human β3 subunit immunoglobulin (Ig) domain, a functionally important component of $Na_{v}$ channels in neurons and cardiomyocytes. Surprisingly, we found that the β3 subunit Ig domain assembles as a trimer in the crystal asymmetric unit. Analytical ultracentrifugation confirmed the presence of Ig domain monomers, dimers, and trimers in free solution, and atomic force microscopy imaging also detected full-length β3 subunit monomers, dimers, and trimers. Mutation of a cysteine residue critical for maintaining the trimer interface destabilized both dimers and trimers. Using fluorescence photoactivated localization microscopy, we detected full-length β3 subunit trimers on the plasma membrane of transfected HEK293 cells. We further show that β3 subunits can bind to more than one site on the $Na_{v}$ 1.5 α subunit and induce the formation of α subunit oligomers, including trimers. Our results suggest a new and unexpected role for the β3 subunits in $Na_{v}$ channel cross-linking and provide new structural insights into some pathological $Na_{v}$ channel mutations.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	15
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-04-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Voltage-Gated Sodium Channel Beta-3 Subunit Chemistry Amino Acid Sequence Binding Sites Cloning, Molecular Crystallization Crystallography, X-Ray Dimerization HEK293 Cells Immunoglobulins Microscopy, Atomic Force Molecular Sequence Data NAV1.5 Voltage-Gated Sodium Channel Protein Conformation Ultracentrifugation Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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