JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on June 29, 2001
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
276/27/24449    most recent
C100184200v1
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 Lopes, C. M. B.
Right arrow Articles by Goldstein, S. A. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lopes, C. M. B.
Right arrow Articles by Goldstein, S. A. N.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print May 17, 2001
J. Biol. Chem, 10.1074/jbc.C100184200
Submitted on April 11, 2001
Revised on May 16, 2001
Accepted on May 16, 2001

Block of Kcnk3 by protons: evidence that 2-P-domain potassium channel subunits function as homodimers

Coeli M. B. Lopes, Noam Zilberberg, and Steve A. N. Goldstein

Pediatrics and Cellular and Molecular Physiology, Yale University, New Haven, CT 06536

Corresponding Author: steve.goldstein{at}yale.edu

KCNK subunits have two pore-forming P domains and four predicted transmembrane segments. To assess the number of subunits in each pore, we studied external proton block of Kcnk3, a subunit prominent in rodent heart and brain. Consistent with a pore blocking mechanism, inhibition was dependent on voltage, potassium concentration, and a histidine in the first P domain (P1H). Thus, at pH 6.8 with 20 mM potassium half the current passed by P1H channels was blocked (apparently via two sites ~10% into the electrical field) whereas channels with an asparagine substitution (P1N) were fully active. Furthermore, pore blockade by barium was sensitive to pH in P1H but not P1N channels. Whereas linking two Kcnk3 subunits in tandem to produce P1H-P1H and P1N-P1N channels bearing four P domains did not alter these attributes, the mixed tandems P1H-P1N and P1N-P1H were half-blocked at pH ~6.4, apparently via a single site. This implicates a dimeric structure for Kcnk3 channels with two (and only two) P1 domains in each pore and argues that P2 domains also contribute to pore formation.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. Cohen, Y. Ben-Abu, S. Hen, and N. Zilberberg
A Novel Mechanism for Human K2P2.1 Channel Gating: FACILITATION OF C-TYPE GATING BY PROTONATION OF EXTRACELLULAR HISTIDINE RESIDUES
J. Biol. Chem., July 11, 2008; 283(28): 19448 - 19455.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. E. Clarke, E. L. Veale, K. Wyse, J. I. Vandenberg, and A. Mathie
The M1P1 Loop of TASK3 K2P Channels Apposes the Selectivity Filter and Influences Channel Function
J. Biol. Chem., June 20, 2008; 283(25): 16985 - 16992.
[Abstract] [Full Text] [PDF]

Home page
 Cardiovasc ResHome page
C. Putzke, K. Wemhoner, F. B. Sachse, S. Rinne, G. Schlichthorl, X. T. Li, L. Jae, I. Eckhardt, E. Wischmeyer, H. Wulf, et al.
The acid-sensitive potassium channel TASK-1 in rat cardiac muscle
Cardiovasc Res, July 1, 2007; 75(1): 59 - 68.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. I. Niemeyer, F. D. Gonzalez-Nilo, L. Zuniga, W. Gonzalez, L. P. Cid, and F. V. Sepulveda
Neutralization of a single arginine residue gates open a two-pore domain, alkali-activated K+ channel
PNAS, January 9, 2007; 104(2): 666 - 671.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
G. W. Abbott, M. H. Butler, and S. A. N. Goldstein
Phosphorylation and protonation of neighboring MiRP2 sites: function and pathophysiology of MiRP2-Kv3.4 potassium channels in periodic paralysis
FASEB J, February 1, 2006; 20(2): 293 - 301.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. J. Morton, A. Abohamed, A. Sivaprasadarao, and M. Hunter
pH sensing in the two-pore domain K+ channel, TASK2
PNAS, November 1, 2005; 102(44): 16102 - 16106.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
A. D O'Connell, M. J Morton, A. Sivaprasadarao, and M. Hunter
Selectivity and interactions of Ba2+ and Cs+ with wild-type and mutant TASK1 K+ channels expressed in Xenopus oocytes
J. Physiol., February 1, 2005; 562(3): 687 - 696.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
C. E Clarke, E. L Veale, P. J Green, H. J Meadows, and A. Mathie
Selective block of the human 2-P domain potassium channel, TASK-3, and the native leak potassium current, IKSO, by zinc
J. Physiol., October 1, 2004; 560(1): 51 - 62.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
R. P. Johnson, I. M. O'Kelly, and I. M. Fearon
System-specific O2 sensitivity of the tandem pore domain K+ channel TASK-1
Am J Physiol Cell Physiol, February 1, 2004; 286(2): C391 - C397.
[Abstract] [Full Text]

Home page
 J. Physiol.Home page
D. Kang, J. Han, E. M. Talley, D. A. Bayliss, and D. Kim
Functional expression of TASK-1/TASK-3 heteromers in cerebellar granule cells
J. Physiol., January 1, 2004; 554(1): 64 - 77.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
I. Lauritzen, M. Zanzouri, E. Honore, F. Duprat, M. U. Ehrengruber, M. Lazdunski, and A. J. Patel
K+-dependent Cerebellar Granule Neuron Apoptosis: ROLE OF TASK LEAK K+ CHANNELS
J. Biol. Chem., August 22, 2003; 278(34): 32068 - 32076.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Physiol.Home page
K. Hui, D. McIntyre, and R. J. French
Conotoxins as Sensors of Local pH and Electrostatic Potential in the Outer Vestibule of the Sodium Channel
J. Gen. Physiol., June 30, 2003; 122(1): 63 - 79.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Interv.Home page
D. A. Bayliss, J. E. Sirois, and E. M. Talley
The TASK Family: Two-Pore Domain Background K+ Channels
Mol. Interv., June 1, 2003; 3(4): 205 - 219.
[Abstract] [Full Text] [PDF]

Home page
 Cardiovasc ResHome page
P. Hajdu, C. Ulens, G. Panyi, and J. Tytgat
Drug- and mutagenesis-induced changes in the selectivity filter of a cardiac two-pore background K+ channel
Cardiovasc Res, April 1, 2003; 58(1): 46 - 54.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Pharmacol.Home page
G. Czirjak and P. Enyedi
Ruthenium Red Inhibits TASK-3 Potassium Channel by Interconnecting Glutamate 70 of the Two Subunits
Mol. Pharmacol., March 1, 2003; 63(3): 646 - 652.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. M. Talley and D. A. Bayliss
Modulation of TASK-1 (Kcnk3) and TASK-3 (Kcnk9) Potassium Channels. VOLATILE ANESTHETICS AND NEUROTRANSMITTERS SHARE A MOLECULAR SITE OF ACTION
J. Biol. Chem., May 10, 2002; 277(20): 17733 - 17742.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
C. P. Washburn, J. E. Sirois, E. M. Talley, P. G. Guyenet, and D. A. Bayliss
Serotonergic Raphe Neurons Express TASK Channel Transcripts and a TASK-Like pH- and Halothane-Sensitive K+ Conductance
J. Neurosci., February 15, 2002; 22(4): 1256 - 1265.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. Czirjak and P. Enyedi
Formation of Functional Heterodimers between the TASK-1 and TASK-3 Two-pore Domain Potassium Channel Subunits
J. Biol. Chem., February 8, 2002; 277(7): 5426 - 5432.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.