ArticleThe Journal of biological chemistry2010
Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- Pasteurella multocida toxin - lessons learned from a mitogenic toxin.Frontiers in immunology · 2022Review
- TheFrontiers in microbiology · 2020Article
- 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
- 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
- Article
- A novel phosphatidylinositol 4,5-bisphosphate binding domain mediates plasma membrane localization of ExoU and other patatin-like phospholipases.The Journal of biological chemistry · 2015Article
- Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin.Biomolecular NMR assignments · 2014Article
- Cytotoxicity of the Vibrio vulnificus MARTX toxin effector DUF5 is linked to the C2A subdomain.Proteins · 2014Article
- Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin.Biomolecular NMR assignments · 2014Article
- What a difference a Dalton makes: bacterial virulence factors modulate eukaryotic host cell signaling systems via deamidation.Microbiology and molecular biology reviews : MMBR · 2013Review
- Pasteurella multocida toxin as a transporter of non-cell-permeating proteins.Infection and immunity · 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
- Plasma membrane association of three classes of bacterial toxins is mediated by a basic-hydrophobic motif.Cellular microbiology · 2012Article
- Bacterial toxin effector-membrane targeting: outside in, then back again.Frontiers in cellular and infection microbiology · 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
- Vibrio vulnificus rtxA1 gene recombination generates toxin variants with altered potency during intestinal infection.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Effector glycosyltransferases in legionella.Frontiers in microbiology · 2011Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pasteurella multocida toxin (PMT) is a virulence factor responsible for the pathogenesis of some forms of pasteurellosis. The toxin activates G(q)- and G(12/13)-dependent pathways through the deamidation of a glutamine residue in the alpha-subunit of heterotrimeric GTPases. We recently reported the crystal structure of the C terminus (residues 575-1285) of PMT (C-PMT), which is composed of three domains (C1, C2, and C3), and that the C1 domain is involved in the localization of C-PMT to the plasma membrane, and the C3 domain possesses a cysteine protease-like catalytic triad. In this study, we analyzed the membrane-targeting function of the C1 domain in detail. The C1 domain consists of seven helices of which the first four (residues 590-670), showing structural similarity to the N terminus of Clostridium difficile toxin B, were found to be involved in the recruitment of C-PMT to the plasma membrane. C-PMT lacking these helices (C-PMT DeltaC1(4H)) neither localized to the plasma membrane nor stimulated the G(q/12/13)-dependent signaling pathways. When the membrane-targeting property was complemented by a peptide tag with an N-myristoylation motif, C-PMT DeltaC1(4H) recovered the PMT activity. Direct binding between the C1 domain and liposomes containing phospholipids was evidenced by surface plasmon resonance analyses. These results indicate that the C1 domain of C-PMT functions as a targeting signal for the plasma membrane.
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