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 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. StoneBackground: 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 CHEMISTRYVolume
288Issue
14Pages
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 BiologyVersion
- 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
2013Notes
This article is closed access.ISSN
0021-9258Publisher version
Language
- en
