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https://hdl.handle.net/10216/114511
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DC Field | Value | Language |
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dc.creator | Almeida, MT | - |
dc.creator | Mesquita, FS | - |
dc.creator | Cruz, R | - |
dc.creator | Osório, H | - |
dc.creator | Custódio, R | - |
dc.creator | Brito, C | - |
dc.creator | Vingadassalom, D | - |
dc.creator | Martins, M | - |
dc.creator | Leong, JM | - |
dc.creator | Holden, DW | - |
dc.creator | Cabanes, D | - |
dc.creator | Sousa, S | - |
dc.date.accessioned | 2018-08-14T15:07:20Z | - |
dc.date.available | 2018-08-14T15:07:20Z | - |
dc.date.issued | 2015 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10216/114511 | - |
dc.description.abstract | Bacterial pathogens often interfere with host tyrosine phosphorylation cascades to control host responses and cause infection. Given the role of tyrosine phosphorylation events in different human infections and our previous results showing the activation of the tyrosine kinase Src upon incubation of cells with Listeria monocytogenes, we searched for novel host proteins undergoing tyrosine phosphorylation upon L. monocytogenes infection. We identify the heavy chain of the non-muscle myosin IIA (NMHC-IIA) as being phosphorylated in a specific tyrosine residue in response to L. monocytogenes infection. We characterize this novel post-translational modification event and show that, upon L. monocytogenes infection, Src phosphorylates NMHC-IIA in a previously uncharacterized tyrosine residue (Tyr-158) located in its motor domain near the ATP-binding site. In addition, we found that other intracellular and extracellular bacterial pathogens trigger NMHC-IIA tyrosine phosphorylation. We demonstrate that NMHC-IIA limits intracellular levels of L. monocytogenes, and this is dependent on the phosphorylation of Tyr-158. Our data suggest a novel mechanism of regulation of NMHC-IIA activity relying on the phosphorylation of Tyr-158 by Src. | - |
dc.description.sponsorship | This work was supported by the Fundo Europeu de Desenvolvimento Regional (FEDER) through the Operational Competitiveness Programme (COMPETE), by National Funds through Fundação para a Ciência e Tecnologia (FCT) under Project PTDC/BIA-BCM/100088/2008FCOMP-01-0124- FEDER-008860 and ERANet-Pathogenomics LISTRESS ERA-PTG/0003/ 2010, Project NORTE-07-0124-FEDER-000002-Host-Pathogen Interactions, co-funded by Programa Operacional Regional do Norte (ON.2-O Novo Norte), under the Quadro de Referência Estratégico Nacional, through FEDER, by FCT, and by a Research Grant 2014 by the European Society of Clinical Microbiology and Infectious Diseases (ESCMID) (to S. S.). M. T. A. received a Travel Grant from Boehringer Ingelheim Fonds. Recipients of Fundação para a Ciência e Tecnologia Doctoral Fellowships BD/43352/2008 and BD/90607/2012. Recipient of EMBO Long Term Post-doctoral Fellowship EMBO ALTF 864-2012. Supported by Ciência 2008 and FCT Investigator Programs COMPETE, POPH, and FCT. | - |
dc.language.iso | eng | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.relation | info:eu-repo/grantAgreement/FCT/5876-PPCDTI/100088/PT | - |
dc.relation | info:eu-repo/grantAgreement/FCT/3599-PPCDT/116472/PT | - |
dc.relation | info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F43352%2F2008/PT | - |
dc.relation | info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F90607%2F2012/PT | - |
dc.relation.ispartof | The Journal of biological chemistry, vol. 290(13), p. 8383-8395 | - |
dc.rights | openAccess | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Bacterial Load | - |
dc.subject | Caco-2 Cells | - |
dc.subject | Enzyme Activation | - |
dc.subject | HeLa Cells | - |
dc.subject | Host-Pathogen Interactions | - |
dc.subject | Humans | - |
dc.subject | Listeria monocytogenes/physiology | - |
dc.subject | Listeriosis/enzymology | - |
dc.subject | Listeriosis/microbiology | - |
dc.subject | Nonmuscle Myosin Type IIA/metabolism | - |
dc.subject | Phosphorylation | - |
dc.subject | Protein Processing, Post-Translational | - |
dc.subject | src-Family Kinases/metabolism | - |
dc.title | Src-dependent tyrosine phosphorylation of non-muscle myosin heavy chain-IIA restricts Listeria monocytogenes cellular infection. | - |
dc.type | Artigo em Revista Científica Internacional | - |
dc.contributor.uporto | Instituto de Investigação e Inovação em Saúde | - |
dc.identifier.doi | 10.1074/jbc.M114.591313 | - |
dc.relation.publisherversion | http://www.jbc.org/content/290/13/8383.long | - |
Appears in Collections: | I3S - Artigo em Revista Científica Internacional |
Files in This Item:
File | Description | Size | Format | |
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Almeida 2015.pdf | 1.75 MB | Adobe PDF | View/Open |
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