Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates

The CagA protein of Helicobacter pylori interacts with numerous cellular factors, and is associated with increased virulence and risk of gastric carcinoma. We present here the co-crystal structure of a subdomain of CagA with the human kinase PAR1b/MARK2, revealing that a CagA peptide mimics substrat...

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Detalles Bibliográficos
Autores principales: Neišić, Dragana, Miller, Marshall C., Quinkert, Zachary T., Stein, Markus, Chait, Brian T., Stebbins, C. Erec
Formato: Texto
Lenguaje:English
Publicado: 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3006182/
https://www.ncbi.nlm.nih.gov/pubmed/19966800
http://dx.doi.org/10.1038/nsmb.1705
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author Neišić, Dragana
Miller, Marshall C.
Quinkert, Zachary T.
Stein, Markus
Chait, Brian T.
Stebbins, C. Erec
author_facet Neišić, Dragana
Miller, Marshall C.
Quinkert, Zachary T.
Stein, Markus
Chait, Brian T.
Stebbins, C. Erec
author_sort Neišić, Dragana
collection PubMed
description The CagA protein of Helicobacter pylori interacts with numerous cellular factors, and is associated with increased virulence and risk of gastric carcinoma. We present here the co-crystal structure of a subdomain of CagA with the human kinase PAR1b/MARK2, revealing that a CagA peptide mimics substrates of this kinase family, resembling eukaryotic protein kinase inhibitors. Mutagenesis of conserved residues central to this interaction renders CagA inactive as an inhibitor of MARK2.
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spelling pubmed-30061822010-12-21 Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates Neišić, Dragana Miller, Marshall C. Quinkert, Zachary T. Stein, Markus Chait, Brian T. Stebbins, C. Erec Nat Struct Mol Biol Article The CagA protein of Helicobacter pylori interacts with numerous cellular factors, and is associated with increased virulence and risk of gastric carcinoma. We present here the co-crystal structure of a subdomain of CagA with the human kinase PAR1b/MARK2, revealing that a CagA peptide mimics substrates of this kinase family, resembling eukaryotic protein kinase inhibitors. Mutagenesis of conserved residues central to this interaction renders CagA inactive as an inhibitor of MARK2. 2009-12-06 2010-01 /pmc/articles/PMC3006182/ /pubmed/19966800 http://dx.doi.org/10.1038/nsmb.1705 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Neišić, Dragana
Miller, Marshall C.
Quinkert, Zachary T.
Stein, Markus
Chait, Brian T.
Stebbins, C. Erec
Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates
title Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates
title_full Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates
title_fullStr Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates
title_full_unstemmed Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates
title_short Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates
title_sort helicobacter pylori caga inhibits par1/mark family kinases by mimicking host substrates
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3006182/
https://www.ncbi.nlm.nih.gov/pubmed/19966800
http://dx.doi.org/10.1038/nsmb.1705
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AT steinmarkus helicobacterpyloricagainhibitspar1markfamilykinasesbymimickinghostsubstrates
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