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PMID: 2536173 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Voltage-gated channels formed in lipid bilayers by a positively charged segment of the Na-channel polypeptide.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 86 ·No. 2 ·1989-01-00 ·Pages 707-10

Tosteson MT, Auld DS, Tosteson DC

Abstract

The Na-channel polypeptide is responsible for the voltage-gated and time-dependent ionic permeability changes that give rise to the action potential in the membranes of nerve cells. We have synthesized a 22-amino acid peptide with a sequence identical to that of the segment named S4, repeat IV of the primary structure of the Na channel. We have found that this peptide induces a voltage- and time-dependent conductance in bilayers formed by a mixture of phosphatidyl-ethanolamine and phosphatidylserine. This conductance is activated when the cis side is made positive, with an apparent gating charge of 3. The results are consistent with the idea that this segment plays a role in determining the voltage sensitivity of the Na channel.

MeSH Terms

Action Potentials Lipid Bilayers/metabolism Peptides/metabolism Sodium Channels/metabolism

Chemicals

Lipid Bilayers Peptides Sodium Channels

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Tosteson M T

Laboratory for Membrane Transport, Harvard Medical School, Boston, MA 02115.

Auld D S

Tosteson D C

References (11)

11 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.86.2.707

Published

1989-01-00

Pages

707-10

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC286543

Subset

Grants

NIGMS NIH HHS · GM25277 · United States

External Links

PubMed source DOI: 10.1073/pnas.86.2.707 PMC Full Text View journal details

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Voltage-gated channels formed in lipid bilayers by a positively charged segment of the Na-channel polypeptide.

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