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    The duffy antigen/receptor for chemokines exists in an oligomeric form in living cells and functionally antagonizes CCR5 signaling through hetero-oligomerization

    Access Status
    Open access via publisher
    Authors
    Chakera, Aron
    Seeber, R.
    John, A.
    Eidne, K.
    Greaves, D.
    Date
    2008
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Chakera, A. and Seeber, R. and John, A. and Eidne, K. and Greaves, D. 2008. The duffy antigen/receptor for chemokines exists in an oligomeric form in living cells and functionally antagonizes CCR5 signaling through hetero-oligomerization. Molecular Pharmacology. 73 (5): pp. 1362-1370.
    Source Title
    Molecular Pharmacology
    DOI
    10.1124/mol.107.040915
    ISSN
    0026-895X
    School
    Curtin Medical School
    URI
    http://hdl.handle.net/20.500.11937/2923
    Collection
    • Curtin Research Publications
    Abstract

    The Duffy antigen/receptor for chemokines (DARC) is an unusual chemokine receptor that binds a large number of inflammatory chemokines of both the CC and CXC families with nanomolar affinity, yet it lacks the ability to signal upon ligand binding. Using bioluminescent resonant energy transfer, we have demonstrated for the first time that DARC exists as a constitutive homo-oligomer in living cells and furthermore that DARC hetero-oligomerizes with the CC chemokine receptor CCR5. DARC-CCR5 interaction impairs chemotaxis and calcium flux through CCR5, whereas internalization of CCR5 in response to ligand binding remains unchanged. These results suggest a novel mechanism by which DARC could modulate inflammatory responses to chemokines in vivo. Copyright © 2008 The American Society for Pharmacology and Experimental Therapeutics.

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