Control of CXCR2 activity through its ubiquitination on K327 residue

@inproceedings{Leclair2014ControlOC,
  title={Control of CXCR2 activity through its ubiquitination on K327 residue},
  author={H{\'e}loise M Leclair and Sonia M Dubois and Sandy Azzi and Julie Dwyer and Nicolas Bid{\`e}re and Julie Gavard},
  booktitle={BMC Cell Biology},
  year={2014}
}
The interleukin-8 chemokine (IL-8) G-protein coupled receptor CXCR2 governs pro-inflammatory and pro-angiogenic responses in leukocytes and endothelial cells. At a molecular standpoint, CXCR2 is widely reported to operate through calcium flux, phosphoinoisitide 3 kinase (PI3K) and mitogen-activated protein kinase (MAPK). While CXCR2 trafficking is suspected to be intertwined with its signaling, the exact mechanism is not fully elucidated. Here, we identified the lysine 327 within the CXCR2 C… CONTINUE READING
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