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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 contribution
posted on 15.09.2015 by Joshua H.Y. Tan, Justin P. Ludeman, Jamie Wedderburn, Meritxell Canals, Pam Hall, Stephen 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.

Funding

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.).

History

School

  • Science

Department

  • Chemistry

Published in

JOURNAL OF BIOLOGICAL CHEMISTRY

Volume

288

Issue

14

Pages

10024 - 10034 (11)

Citation

TAN, 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

Version

VoR (Version of Record)

Publisher statement

This 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/

Publication date

2013

Notes

This article is closed access.

ISSN

0021-9258

Language

en

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