WWW.JNEUROSCI.ORG
-
The Journal of Neuroscience Fine Science Tools - Extraordinary Craftsmanship
 QUICK SEARCH:   [advanced]


     
-


HOME
  |  
SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

This Article
Right arrow Full Text (PDF)
Right arrow Submit an eLetter
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Blumenthal, E. M.
Right arrow Articles by Kaczmarek, L. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Blumenthal, E. M.
Right arrow Articles by Kaczmarek, L. K.

 Previous Article  |  Next Article 

Journal of Neuroscience, Vol 14, 3097-3105, Copyright © 1994 by Society for Neuroscience


ARTICLE

The minK potassium channel exists in functional and nonfunctional forms when expressed in the plasma membrane of Xenopus oocytes

EM Blumenthal and LK Kaczmarek
Interdepartmental Neuroscience Program, Yale University School of Medicine, New Haven, Connecticut 06510.

The minK protein induces a slowly activating voltage-dependent potassium current when expressed in Xenopus oocytes. In order to measure the levels of minK protein in the plasma membrane, we have modified the minK gene by inserting a 9 amino acid epitope into the N- terminal domain of the protein sequence. When intact live oocytes are injected with the modified minK RNA and subsequently incubated with an antibody to this epitope, specific binding is detected, indicating that the N-terminal domain is extracellular. We found that when oocytes are injected with amounts of minK mRNA up to 50 ng, the levels of protein at the surface are proportional to the amount of injected mRNA. In contrast, the amplitude of the minK current recorded in the oocytes saturates at 1 ng of injected mRNA. Although the amplitude of the currents is not altered by increasing mRNA levels above 1 ng, the kinetics of activation of the current differ in oocytes with high or low levels of minK RNA. In particular, activation is slower with higher levels of minK protein in the plasma membrane. Finally, we find that increasing intracellular cAMP levels, which increases the amplitude of minK currents, does not alter surface expression of the minK protein but produces a small increase in the rate of activation of the current. Our results support a model in which minK protein forms functional potassium channels by association with a factor endogenous to the oocyte.


This article has been cited by other articles:


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
X.-S. Liu, M. Jiang, M. Zhang, D. Tang, H. F. Clemo, R. S. D. Higgins, and G.-N. Tseng
Electrical remodeling in a canine model of ischemic cardiomyopathy
Am J Physiol Heart Circ Physiol, January 1, 2007; 292(1): H560 - H571.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
J.-Y. Park, H.-W. Kang, H.-J. Moon, S.-U. Huh, S.-W. Jeong, N. M. Soldatov, and J.-H. Lee
Activation of protein kinase C augments T-type Ca2+ channel activity without changing channel surface density
J. Physiol., December 1, 2006; 577(2): 513 - 523.
[Abstract] [Full Text] [PDF]


Home page
Cardiovasc ResHome page
V. Trepanier-Boulay, M.-A. Lupien, C. St-Michel, and C. Fiset
Postnatal development of atrial repolarization in the mouse
Cardiovasc Res, October 1, 2004; 64(1): 84 - 93.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
R. Warth and J. Barhanin
The multifaceted phenotype of the knockout mouse for the KCNE1 potassium channel gene
Am J Physiol Regulatory Integrative Comp Physiol, March 1, 2002; 282(3): R639 - R648.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
U. C. Hoppe, E. Marban, and D. C. Johns
Distinct gene-specific mechanisms of arrhythmia revealed by cardiac gene transfer of two long QT disease genes, HERG and KCNE1
PNAS, April 24, 2001; 98(9): 5335 - 5340.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
W. Wang, J. Xia, and R. S. Kass
MinK-KvLQT1 Fusion Proteins, Evidence for Multiple Stoichiometries of the Assembled IsK Channel
J. Biol. Chem., December 18, 1998; 273(51): 34069 - 34074.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
G. Romey, B. Attali, C. Chouabe, I. Abitbol, E. Guillemare, J. Barhanin, and M. Lazdunski
Molecular Mechanism and Functional Significance of the MinK Control of the KvLQT1 Channel Activity
J. Biol. Chem., July 4, 1997; 272(27): 16713 - 16716.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K.-K. Tai, K.-W. Wang, and S. A.N. Goldstein
MinK Potassium Channels Are Heteromultimeric Complexes
J. Biol. Chem., January 17, 1997; 272(3): 1654 - 1658.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. Ben-Efraim, Y. Shai, and B. Attali
Cytoplasmic and Extracellular IsK Peptides Activate Endogenous K[IMAGE] and Cl[IMAGE] Channels in Xenopus Oocytes
J. Biol. Chem., April 12, 1996; 271(15): 8768 - 8771.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
T. Yang, S. Kupershmidt, and D. M. Roden
Anti-minK Antisense Decreases the Amplitude of the Rapidly Activating Cardiac Delayed Rectifier K+ Current
Circ. Res., December 1, 1995; 77(6): 1246 - 1253.
[Abstract] [Full Text]


Home page
Circ. Res.Home page
H. J. Duff, Z.-P. Feng, and R. S. Sheldon
High- and Low-Affinity Sites for [3H]Dofetilide Binding to Guinea Pig Myocytes
Circ. Res., October 1, 1995; 77(4): 718 - 725.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
G. Levin, T. Keren, T. Peretz, D. Chikvashvili, W. B. Thornhill, and I. Lotan
Regulation of RCK1 Currents with a cAMP Analog via Enhanced Protein Synthesis and Direct Channel Phosphorylation
J. Biol. Chem., June 16, 1995; 270(24): 14611 - 14618.
[Abstract] [Full Text] [PDF]



-

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help

-
Copyright 2009 by Society for Neuroscience ONLINE ISSN: 1529-2401
-