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


     

Published online before print March 27, 2008
Protein Science, DOI: 10.1110/ps.083445408
 Copyright © 2008 The Protein Society
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Research Data
Right arrow All Versions of this Article:
ps.083445408v1
17/5/945    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 Google Scholar
Google Scholar
Right arrow Articles by Aminova, L. R.
Right arrow Articles by Wilson, B. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Aminova, L. R.
Right arrow Articles by Wilson, B. A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

FOR THE RECORD

The C3 domain of Pasteurella multocida toxin is the minimal domain responsible for activation of Gq-dependent calcium and mitogenic signaling

Leila R. Aminova, Shuhong Luo, Yuka Bannai, Mengfei Ho, and Brenda A. Wilson

Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA

(RECEIVED January 8, 2008; FINAL REVISION February 9, 2008; ACCEPTED February 9, 2008)

The large 1285-amino-acid protein toxin from Pasteurella multocida (PMT) is a multifunctional single-chain polypeptide that binds to and enters eukaryotic cells and acts intracellularly to promote Gq and G12/13 protein-dependent calcium and mitogenic signal transduction. Previous studies indicated that the intracellular activity domain responsible for PMT action was located within the C-terminal 600–700 amino acids. In this study, we have exogenously expressed a series of N- and C-terminal PMT fragments directly in mammalian cells and have used the dual luciferase reporter system to assay for toxin-mediated activation of calcium-calcineurin-NFAT signaling (NFAT-luciferase) and mitogenic serum response signaling (SRE-luciferase). Using this approach, we have defined the last 180 amino acids, which encompass the C3 domain in the crystal structure, as the minimum domain sufficient to activate both NFAT and SRE signaling pathways.

Keywords: dermonecrotic toxin; NFAT; SRE; calcium mobilization; Gq protein

Supplemental material: see www.proteinscience.org

Reprint requests to: Brenda A. Wilson, Department of Microbiology, University of Illinois at Urbana-Champaign, 601 South Goodwin Avenue, B128 CLSL, Urbana, Illinois 61801, USA; e-mail: bawilson{at}life.uiuc.edu; fax: (217) 244-6697.

Abbreviations: rPMT, recombinant Pasteurella multocida toxin; NFAT, nuclear factor of activated T cells; SRE, serum response element; PLC, phospholipase C; PKC, protein kinase C.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.083445408.


Add to CiteULike CiteULike   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?




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2008 by The Protein Society.