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, 13:59authored byJoshua 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.
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.
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