Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker.

Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker. Research Abstract Details 

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Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker. Abstract Text:

James R Groome,Margaret C Dice,Esther Fujimoto,Peter C Ruben,

We investigated structural determinants of fast inactivation and deactivation in sodium channels by comparing ionic flux and charge movement in skeletal muscle channels, using mutations of DIII-DIV linker charges. Charge altering and substituting mutations at K-1317, K-1318 depolarized the g(V) curve but hyperpolarized the h(infinity) curve. Charge reversal and substitution at this locus reduced the apparent voltage sensitivity of open- and closed-state fast inactivation. These effects were not observed with charge reversal at E-1314, E-1315. Mutations swapping or neutralizing the negative cluster at 1314, 1315 and the positive cluster at 1317, 1318 indicated that local interactions dictate the coupling of activation to fast inactivation. Gating charge was immobilized before channel entry into fast inactivation in hNa(V)1.4 but to a lesser extent in mutations at K-1317, K-1318. These results suggest that charge is preferentially immobilized in channels inactivating from the open state. Recovery of gating charge proceeded with a single, fast phase in the double mutation K-1317R, K-1318R. This mutation also partially uncoupled recovery from deactivation. Our findings indicate that charged residues near the fast inactivation "particle" allosterically interact with voltage sensors to control aspects of gating in sodium channels.

Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker. Publishing Authors By Initials

JR Groome,MC Dice,E Fujimoto,PC Ruben,

For similar animals: chordata: vertebrates: amphibia: anura: pipidae: xenopus: xenopus laevis research abstracts see: animals: chordata: vertebrates: amphibia: anura: pipidae: xenopus: xenopus laevis research

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Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Biophysical journal

VOLUME: 93

Page Numbers: 1519-33

Journal Abbreviation: Biophys. J.

ISSN: 0006-3495

DAY: 18

MONTH: 05

YEAR: 2007

Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370626

Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker. Keywords Mesh Terms:

KEYWORDS: Xenopus laevis

MESH TERMS: chemistry

Chemical & Substance for Abstract: Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker. Information

Substance Name: Sodium

Registry Number: 7440-23-5

Grant and Affiliation Information for Charge immobilization of skeletal muscle Na+ channels: role of residues in the inactivation linker.

AFFILIATION: Department of Biological Sciences, Idaho State University, Pocatello, ID 83209-8007, USA. groojame@isu.edu

Country: United States

AGENCY: United States NINDS

GRANT: R01 NS29204

ACRONYM: NS

MEDLINETA: Biophys J

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