ArticleProtein science : a publication of the Protein Society2008
The C3 domain of Pasteurella multocida toxin is the minimal domain responsible for activation of Gq-dependent calcium and mitogenic signaling.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 26 citations in OpenAlex.
- The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling.Science signaling · 2018Article
- Cytosolic Delivery of Multidomain Cargos by the N Terminus of Pasteurella multocida Toxin.Infection and immunity · 2018Article
- Modular domain swapping among the bacterial cytotoxic necrotizing factor (CNF) family for efficient cargo delivery into mammalian cells.The Journal of biological chemistry · 2018Article
- The membrane localization domains of two distinct bacterial toxins form a 4-helix-bundle in solution.Protein science : a publication of the Protein Society · 2017Article
- Selective Membrane Redistribution and Depletion of Gαq-Protein by Pasteurella multocida Toxin.Toxins · 2016Article
- Cytotoxicity of the Vibrio vulnificus MARTX toxin effector DUF5 is linked to the C2A subdomain.Proteins · 2014Article
- Determinants of pH-dependent modulation of translocation in dermonecrotic G-protein-deamidating toxins.Toxins · 2013Article
- Pasteurella multocida toxin (PMT) upregulates CTGF which leads to mTORC1 activation in Swiss 3T3 cells.Cellular signalling · 2013Article
- Substrate specificity of Pasteurella multocida toxin for α subunits of heterotrimeric G proteins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013Article
- Identification and characterization of monoclonal antibodies against the ORFV059 protein encoded by Orf virus.Virus genes · 2012Article
- Rho/ROCK-dependent inhibition of 3T3-L1 adipogenesis by G-protein-deamidating dermonecrotic toxins: differential regulation of Notch1, Pref1/Dlk1, and β-catenin signaling.Frontiers in cellular and infection microbiology · 2012Article
- Pasteurella multocida toxin interaction with host cells: entry and cellular effects.Current topics in microbiology and immunology · 2012Review
- Cellular and molecular action of the mitogenic protein-deamidating toxin from Pasteurella multocida.The FEBS journal · 2011Review
- Membrane interaction of Pasteurella multocida toxin involves sphingomyelin.The FEBS journal · 2011Article
- Article
- Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.Future microbiology · 2010Review
- Identification of a conserved membrane localization domain within numerous large bacterial protein toxins.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Pasteurella multocida toxin activates various heterotrimeric G proteins by deamidation.Toxins · 2010Article
- Protease activated receptor signaling is required for African trypanosome traversal of human brain microvascular endothelial cells.PLoS neglected tropical diseases · 2009Article
- Pasteurella multocida toxin activation of heterotrimeric G proteins by deamidation.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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5 authors at 1 institution in 1 country.
Funding
Abstract
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 G(q) and G(12/13) 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.
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