Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Sci. STKE, 5 October 2004
Vol. 2004, Issue 253, p. re15
[DOI: 10.1126/stke.2532004re15]
REVIEWS
The VGL-Chanome: A Protein Superfamily Specialized for Electrical Signaling and Ionic Homeostasis
Frank H. Yu and
William A. Catterall1*
1Department of Pharmacology, Mailstop 357280, University of Washington, Seattle, WA 981957280, USA.
Abstract:
Complex multicellular organisms require rapid and accurate transmission of information among cells and tissues and tight coordination of distant functions. Electrical signals and resulting intracellular calcium transients, in vertebrates, control contraction of muscle, secretion of hormones, sensation of the environment, processing of information in the brain, and output from the brain to peripheral tissues. In nonexcitable cells, calcium transients signal many key cellular events, including secretion, gene expression, and cell division. In epithelial cells, huge ion fluxes are conducted across tissue boundaries. All of these physiological processes are mediated in part by members of the voltage-gated ion channel protein superfamily. This protein superfamily of 143 members is one of the largest groups of signal transduction proteins, ranking third after the G proteincoupled receptors and the protein kinases in number. Each member of this superfamily contains a similar pore structure, usually covalently attached to regulatory domains that respond to changes in membrane voltage, intracellular signaling molecules, or both. Eight families are included in this protein superfamilyvoltage-gated sodium, calcium, and potassium channels; calcium-activated potassium channels; cyclic nucleotidemodulated ion channels; transient receptor potential (TRP) channels; inwardly rectifying potassium channels; and two-pore potassium channels. This article identifies all of the members of this protein superfamily in the human genome, reviews the molecular and evolutionary relations among these ion channels, and describes their functional roles in cell physiology.
Citation: F. H. Yu, W. A. Catterall, The VGL-Chanome: A Protein Superfamily Specialized for Electrical Signaling and Ionic Homeostasis. Sci. STKE2004, re15 (2004).
Richard Horn (25 October 2005) Sci. STKE2005 (307), pe50.
[DOI: 10.1126/stke.3072005pe50] |Abstract »|Full Text »|PDF »
PERSPECTIVES
Maria L. Garcia and Gregory J. Kaczorowski (20 September 2005) Sci. STKE2005 (302), pe46.
[DOI: 10.1126/stke.stke.3022005pe46] |Abstract »|Full Text »|PDF »
Matthew Fury, Steven O. Marx, and Andrew R. Marks (12 March 2002) Sci. STKE2002 (123), pe12.
[DOI: 10.1126/stke.2002.123.pe12] |Abstract »|Full Text »|PDF »
REVIEWS
Donald W. Hilgemann, Siyi Feng, and Cem Nasuhoglu (4 December 2001) Sci. STKE2001 (111), re19.
[DOI: 10.1126/stke.2001.111.re19] |Gloss »|Abstract »|Full Text »|PDF »|Erratum »
Hyperpolarization-Activated Cation Channels: From Genes to Function.
M. Biel, C. Wahl-Schott, S. Michalakis, and X. Zong (2009)
Physiol Rev
89, 847-885
|Abstract »|Full Text »|PDF »
Inherited Neuronal Ion Channelopathies: New Windows on Complex Neurological Diseases.
W. A. Catterall, S. Dib-Hajj, M. H. Meisler, and D. Pietrobon (2008)
J. Neurosci.
28, 11768-11777
|Abstract »|Full Text »|PDF »
Multiple Unbiased Prospective Screens Identify TRP Channels and Their Conserved Gating Elements.
B. R. Myers, Y. Saimi, D. Julius, and C. Kung (2008)
J. Gen. Physiol.
132, 481-486
|Full Text »|PDF »
Localization and Targeting of Voltage-Dependent Ion Channels in Mammalian Central Neurons.
H. Vacher, D. P. Mohapatra, and J. S. Trimmer (2008)
Physiol Rev
88, 1407-1447
|Abstract »|Full Text »|PDF »
Ion Channels as Drug Targets: The Next GPCRs.
G. J. Kaczorowski, O. B. McManus, B. T. Priest, and M. L. Garcia (2008)
J. Gen. Physiol.
131, 399-405
|Full Text »|PDF »
Vasopressin-induced membrane trafficking of TRPC3 and AQP2 channels in cells of the rat renal collecting duct.
M. Goel, W. G. Sinkins, C.-D. Zuo, U. Hopfer, and W. P. Schilling (2007)
Am J Physiol Renal Physiol
293, F1476-F1488
|Abstract »|Full Text »|PDF »
Putting an end to DEND: A severe neonatal-onset epilepsy is treatable if recognized early.
E. C. Cooper and Z. Pan (2007)
Neurology
69, 1310-1311
|Full Text »|PDF »
Receptor-induced Activation of Drosophila TRP{gamma} by Polyunsaturated Fatty Acids.
S. Jors, V. Kazanski, A. Foik, D. Krautwurst, and C. Harteneck (2006)
J. Biol. Chem.
281, 29693-29702
|Abstract »|Full Text »|PDF »
Voltage sensor conformations in the open and closed states in ROSETTA structural models of K+ channels.
V. Yarov-Yarovoy, D. Baker, and W. A. Catterall (2006)
PNAS
103, 7292-7297
|Abstract »|Full Text »|PDF »
Identification and localization of TRPC channels in the rat kidney.
M. Goel, W. G. Sinkins, C.-D. Zuo, M. Estacion, and W. P. Schilling (2006)
Am J Physiol Renal Physiol
290, F1241-F1252
|Abstract »|Full Text »|PDF »
Separate Populations of Receptor Cells and Presynaptic Cells in Mouse Taste Buds.
R. A. DeFazio, G. Dvoryanchikov, Y. Maruyama, J. W. Kim, E. Pereira, S. D. Roper, and N. Chaudhari (2006)
J. Neurosci.
26, 3971-3980
|Abstract »|Full Text »|PDF »
A common ankyrin-G-based mechanism retains KCNQ and NaV channels at electrically active domains of the axon..
Z. Pan, T. Kao, Z. Horvath, J. Lemos, J.-Y. Sul, S. D. Cranstoun, V. Bennett, S. S. Scherer, and E. C. Cooper (2006)
J. Neurosci.
26, 2599-2613
|Abstract »|Full Text »|PDF »
Upregulation of the Voltage-Gated Sodium Channel {beta}2 Subunit in Neuropathic Pain Models: Characterization of Expression in Injured and Non-Injured Primary Sensory Neurons.
M. Pertin, R.-R. Ji, T. Berta, A. J. Powell, L. Karchewski, S. N. Tate, L. L. Isom, C. J. Woolf, N. Gilliard, D. R. Spahn, et al. (2005)
J. Neurosci.
25, 10970-10980
|Abstract »|Full Text »|PDF »
Reversed voltage-dependent gating of a bacterial sodium channel with proline substitutions in the S6 transmembrane segment.