FASEB J. Pierce now sold as Thermo Scientific
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rehm, H.
Right arrow Articles by Tempel, B. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rehm, H.
Right arrow Articles by Tempel, B. L.

The FASEB Journal, Vol 5, 164-170, Copyright © 1991 by The Federation of American Societies for Experimental Biology

REVIEWS

Voltage-gated K+ channels of the mammalian brain

H Rehm and BL Tempel
Pharmakologisches Institut, Universitat Zurich, Switzerland.

Research on voltage-gated K+ channels of the mammalian brain has seen a flood of new data in the last 2 years. A genetic approach, based on the Shaker mutation of Drosophila, led to cDNA clones for mammalian voltage- gated K+ channels. K+ channel proteins were detected independently and purified with the help of channel specific toxins. From these studies the structure of two families of mammalian K+ channels emerged. One family is defined molecularly by the sequence homology of its members, the other by binding sites for the snake toxin dendrotoxin. The two families have several members in common. The voltage-gated K+ channels of mammalian brain are oligomers of glycosilated peptides of 65-95 kDa. The primary structure of these subunits is characterized by six to eight potential transmembrane regions, including the S4 region, the voltage-sensor of the channels. Associated with at least some K+ channels are 38- and 42-kDa peptides of unknown function. The channels give rise to non- or slow-inactivating K+ currents that are regulated through phosphorylation by both cAMP-dependent and an endogenous kinase.


This article has been cited by other articles:


Home page
 J. Neurosci.Home page
S. S. Sidach and I. M. Mintz
Low-Affinity Blockade of Neuronal N-Type Ca Channels by the Spider Toxin omega -Agatoxin-IVA
J. Neurosci., October 1, 2000; 20(19): 7174 - 7182.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
J. E. Engel and C.-F. Wu
Genetic Dissection of Functional Contributions of Specific Potassium Channel Subunits in Habituation of an Escape Circuit in Drosophila
J. Neurosci., March 15, 1998; 18(6): 2254 - 2267.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
F. M. Kuenzi and N. Dale
The Pharmacology and Roles of two K+ Channels in Motor Pattern Generation in the Xenopus Embryo
J. Neurosci., February 15, 1998; 18(4): 1602 - 1612.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
N. Meiri, C. Ghelardini, G. Tesco, N. Galeotti, D. Dahl, D. Tomsic, S. Cavallaro, A. Quattrone, S. Capaccioli, A. Bartolini, et al.
Reversible antisense inhibition of Shaker-like Kv1.1 potassium channel expression impairs associative memory in mouse and rat
PNAS, April 29, 1997; 94(9): 4430 - 4434.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1991 by The Federation of American Societies for Experimental Biology.