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PMID: 2474407 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Electrical and biochemical properties of the cGMP-gated cation channel from rod photoreceptors.

Cold Spring Harbor symposia on quantitative biology ·Vol. 53 Pt 1 ·1988-00-00 ·Pages 407-15

Kaupp UB, Hanke W, Simmoteit R, Lühring H

Abstract

The light-sensitive channel in the surface membrane of vertebrate photoreceptors is gated directly and cooperatively by cGMP, and the activation mechanism does not involve phosphorylation by a cGMP-dependent protein kinase. The channel protein most likely is composed of several copies of a single type of polypeptide, which can be removed from photoreceptor membranes by detergents and functionally reincorporated into the membrane of liposomes or planar bilayers. Most channel properties are preserved in the reconstituted system and provide a unique system to study the mechanisms of activation, regulation, and ion permeation in more detail.

MeSH Terms
Animals Cyclic GMP/antagonists & inhibitors,pharmacology,physiology Ion Channels/physiology Membrane Potentials Photoreceptor Cells/physiology Signal Transduction
Chemicals
Ion Channels Cyclic GMP
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kaupp U B
Abteilung Biophysik, Universität Osnabrück, Federal Republic of Germany.
Hanke W
Simmoteit R
Lühring H
Article Info
Journal
Cold Spring Harbor symposia on quantitative biology
Abbr.
Cold Spring Harb Symp Quant Biol
ISSN
0091-7451
Published
1988-00-00
Pages
407-15
Language
English
Region
United States
NLM ID
1256107
Subset
IM
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