spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online 3 June 2003
doi: 10.1242/jcs.00595

This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.00595v1
116/14/2967    most recent
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 Miller, L. C.
Right arrow Articles by Braun, J. E. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Miller, L. C.
Right arrow Articles by Braun, J. E. A.
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   Add to Twitter  
What's this?
Journal of Cell Science 116, 2967-2974 (2003)
doi: 10.1242/jcs.00595

Research Article

Molecular determinants of cysteine string protein modulation of N-type calcium channels

Linda C. Miller1,*, Leigh Anne Swayne1,*, Jason G. Kay1, Zhong-Ping Feng1,2, Scott E. Jarvis1, Gerald W. Zamponi1 and Janice E. A. Braun1,{ddagger}

1 Neuroscience Research Group, Department of Physiology and Biophysics, University of Calgary, Calgary, Alberta, T2N 4N1, Canada
2 NeuroMed Technologies Inc., Suite 301, Don Rix Building, 2389 Health Sciences Mall, UBC, Vancouver, BC, V6T 1Z4, Canada

{ddagger} Author for correspondence (e-mail: braunj{at}ucalgary.ca)

Accepted 3 April 2003

Cysteine string proteins (CSPs) are secretory vesicle chaperones that are important for neurotransmitter release. We have previously reported an interaction of CSP with both heterotrimeric GTP-binding proteins (G proteins) and N-type calcium channels that results in a tonic G protein inhibition of the channels. In this report we directly demonstrate that two separate regions of CSP associate with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G{alpha} subunits but not G{alpha}ß subunits whereas the C terminal binding site of CSP associates with either free G{alpha}ß subunits or G{alpha}ß in complex with G{alpha}. The interaction of either binding site of CSP (CSP1-82 or CSP83-198) with G proteins elicits robust tonic inhibition of N-type calcium channel activity. However, CSP1-82 inhibition and CSP83-198 inhibition of calcium channels occur through distinct mechanisms. Calcium channel inhibition by CSP83-198 (but not CSP1-82) is completely blocked by co-expression of the synaptic protein interaction site (synprint) of the N-type channel, indicating that CSP83-198 inhibition is dependent on a physical interaction with the calcium channel. These results suggest that distinct binding sites of CSP can play a role in modulating G protein function and G protein inhibition of calcium channels.

Key words: Cysteine string protein, Chaperones, G proteins, N-type-calcium channels, Synaptic transmission, J domain


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   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
N. Weng, M. D. Baumler, D. D. H. Thomas, M. A. Falkowski, L. A. Swayne, J. E. A. Braun, and G. E. Groblewski
Functional role of J domain of cysteine string protein in Ca2+-dependent secretion from acinar cells
Am J Physiol Gastrointest Liver Physiol, May 1, 2009; 296(5): G1030 - G1039.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. J. Dupre, M. Robitaille, M. Richer, N. Ethier, A. M. Mamarbachi, and T. E. Hebert
Dopamine Receptor-interacting Protein 78 Acts as a Molecular Chaperone for G{gamma} Subunits before Assembly with Gbeta
J. Biol. Chem., May 4, 2007; 282(18): 13703 - 13715.
[Abstract] [Full Text] [PDF]

Home page
 Pharmacol. Rev.Home page
H. W. Tedford and G. W. Zamponi
Direct G Protein Modulation of Cav2 Calcium Channels
Pharmacol. Rev., December 1, 2006; 58(4): 837 - 862.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Natochin, T. N. Campbell, B. Barren, L. C. Miller, S. Hameed, N. O. Artemyev, and J. E. A. Braun
Characterization of the G{alpha}s Regulator Cysteine String Protein
J. Biol. Chem., August 26, 2005; 280(34): 30236 - 30241.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
P. Bronk, Z. Nie, M. K. Klose, K. Dawson-Scully, J. Zhang, R. M. Robertson, H. L. Atwood, and K. E. Zinsmaier
The Multiple Functions of Cysteine-String Protein Analyzed at Drosophila Nerve Terminals
J. Neurosci., March 2, 2005; 25(9): 2204 - 2214.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. C. Miller, L. A. Swayne, L. Chen, Z.-P. Feng, J. L. Wacker, P. J. Muchowski, G. W. Zamponi, and J. E. A. Braun
Cysteine String Protein (CSP) Inhibition of N-type Calcium Channels Is Blocked by Mutant Huntingtin
J. Biol. Chem., December 26, 2003; 278(52): 53072 - 53081.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2003