Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/114511
Author(s): Almeida, MT
Mesquita, FS
Cruz, R
Osório, H
Custódio, R
Brito, C
Vingadassalom, D
Martins, M
Leong, JM
Holden, DW
Cabanes, D
Sousa, S
Title: Src-dependent tyrosine phosphorylation of non-muscle myosin heavy chain-IIA restricts Listeria monocytogenes cellular infection.
Publisher: American Society for Biochemistry and Molecular Biology
Issue Date: 2015
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.
Subject: Amino Acid Sequence
Bacterial Load
Caco-2 Cells
Enzyme Activation
HeLa Cells
Host-Pathogen Interactions
Humans
Listeria monocytogenes/physiology
Listeriosis/enzymology
Listeriosis/microbiology
Nonmuscle Myosin Type IIA/metabolism
Phosphorylation
Protein Processing, Post-Translational
src-Family Kinases/metabolism
URI: http://hdl.handle.net/10216/114511
Source: The Journal of biological chemistry, vol. 290(13), p. 8383-8395
Related Information: info:eu-repo/grantAgreement/FCT/5876-PPCDTI/100088/PT
info:eu-repo/grantAgreement/FCT/3599-PPCDT/116472/PT
info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F43352%2F2008/PT
info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F90607%2F2012/PT
Document Type: Artigo em Revista Científica Internacional
Rights: openAccess
Appears in Collections:I3S - Artigo em Revista Científica Internacional

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