Advertisement
JBC

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


     

A more recent version of this article appeared on April 28, 2006
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
281/17/11769    most recent
M513125200v1
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ren, Y.
Right arrow Articles by Anderson, A. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ren, Y.
Right arrow Articles by Anderson, A. E.
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 March 2, 2006
J. Biol. Chem, 10.1074/jbc.M513125200
Submitted on December 8, 2005
Revised on February 28, 2006
Accepted on March 2, 2006

Regulation of surface localization of the small-conductance CA2+-activated potassium channel, SK2 through direct phosphorylation by cylic amp-dependent protein kinase

Yajun Ren, Barnwell F. Lyndon, Jon C. Alexander, Farah D. Lubin, John P. Adelman, Paul J. Pfaffinger, Laura A. Schrader, and Anne E. Anderson

Pediatric-Neurology, Baylor College of Medicine, Houston, TX 77030

Corresponding Author: annea{at}bcm.tmc.edu

Small conductance, Ca2+-activated voltage-independent potassium channels (SK channels) are widely expressed in diverse tissues; however, little is known about the molecular regulation of SK channel subunits. Direct alteration of ion channel subunits by kinases is a candidate mechanism for functional modulation of these channels. We find that activation of cyclic AMP-dependent protein kinase (PKA) with forskolin (50 µM) causes a dramatic decrease in surface localization of the SK2 channel subunit expressed in COS7 cells due to direct phosphorylation of the SK2 channel subunit. PKA phosphorylation studies using the intracellular domains of the SK2 channel subunit expressed as glutathione S-transferase fusion protein constructs showed that both the amino-terminal (NT) and carboxyl-terminal (CT) regions are PKA substrates in vitro. Mutational analysis identified a single PKA phosphorylation site within the NT of the SK2 subunit at serine (S) 136. Mutagenesis and mass spectrometry studies identified four PKA phosphorylation sites: S465 (minor site) and three amino acid residues S568, S569, S570 (major sites) within the CT region. A mutated SK2 channel subunit, with the three contiguous serines mutated to alanines to block phosphorylation at these sites, shows no decrease in surface expression after PKA stimulation. Thus, our findings suggest that PKA phosphorylation of these three sites is necessary for PKA-mediated reorganization of SK2 surface expression.


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. Neurosci.Home page
E. S. L. Faber, A. J. Delaney, J. M. Power, P. L. Sedlak, J. W. Crane, and P. Sah
Modulation of SK Channel Trafficking by Beta Adrenoceptors Enhances Excitatory Synaptic Transmission and Plasticity in the Amygdala
J. Neurosci., October 22, 2008; 28(43): 10803 - 10813.
[Abstract] [Full Text] [PDF]

Home page
 NeuroscientistHome page
J. Kim and D. A. Hoffman
Potassium Channels: Newly Found Players in Synaptic Plasticity
Neuroscientist, June 1, 2008; 14(3): 276 - 286.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
D. D. Vadysirisack, E. S.-W. Chen, Z. Zhang, M.-D. Tsai, G.-D. Chang, and S. M. Jhiang
Identification of in Vivo Phosphorylation Sites and Their Functional Significance in the Sodium Iodide Symporter
J. Biol. Chem., December 21, 2007; 282(51): 36820 - 36828.
[Abstract] [Full Text] [PDF]

Home page
 Cardiovasc ResHome page
N. Ozgen, W. Dun, E. A. Sosunov, E. P. Anyukhovsky, M. Hirose, H. S. Duffy, P. A. Boyden, and M. R. Rosen
Early electrical remodeling in rabbit pulmonary vein results from trafficking of intracellular SK2 channels to membrane sites
Cardiovasc Res, September 1, 2007; 75(4): 758 - 769.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
L. D. Ellis, W. H. Mehaffey, E. Harvey-Girard, R. W. Turner, L. Maler, and R. J. Dunn
SK Channels Provide a Novel Mechanism for the Control of Frequency Tuning in Electrosensory Neurons
J. Neurosci., August 29, 2007; 27(35): 9491 - 9502.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
X. Cai, D.-S. Wei, S. E. Gallagher, A. Bagal, Y.-A. Mei, J. P. Y. Kao, S. M. Thompson, and C.-M. Tang
Hyperexcitability of Distal Dendrites in Hippocampal Pyramidal Cells after Chronic Partial Deafferentation
J. Neurosci., January 3, 2007; 27(1): 59 - 68.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement