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Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1).
journal contributionposted on 2015-09-15, 13:59 authored by Joshua H.Y. Tan, Justin P. Ludeman, Jamie Wedderburn, Meritxell Canals, Pam Hall, Stephen ButlerStephen Butler, Deni Taleski, Arthur Christopoulos, Michael J. Hickey, Richard J. Payne, Martin J. Stone
Background: Chemokine receptors are post-translationally sulfated on tyrosine residues. Results: A tyrosine-sulfated fragment of CCR2 binds more tightly to the monomeric form than the dimeric form of the chemokine MCP-1. Conclusion: Binding to sulfated CCR2 promotes conversion of MCP-1 from inactive dimer to active monomer. Significance: Tyrosine sulfation may regulate the ability of chemokine receptors to be activated by chemokines.
This work was supported by Australian Research Council Grants DP0881570 and LE0989504 (to M. J. S.) and DP1094884 (to R. J. P. and M. J. S.) and by Australian National Health and Medical Research Council Grant 519461 (to A. C.).
Published inJOURNAL OF BIOLOGICAL CHEMISTRY
Pages10024 - 10034 (11)
CitationTAN, J.H.Y. ... et al, 2013. Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1). Journal of Biological Chemistry, 288 (14), pp. 10024 - 10034.
Publisher© American Society for Biochemistry and Molecular Biology
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Publisher statementThis work is made available according to the conditions of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) licence. Full details of this licence are available at: https://creativecommons.org/licenses/by-nc-nd/4.0/
NotesThis article is closed access.