Title : The role of post-translational modifications of the
CXCR4 amino
terminus in stromal-derived
factor 1 1 alpha association and HIV-1 entry
Abstract :
- The chemokine receptor CXCR4 plays critical roles in development, immune function, and human immunodeficiency virus type 1 (HIV-1) entry
- Here we demonstrate that, like the CC-chemokine receptors CCR5 and CCR2b , CXCR4 is posttranslationally modified by sulfation of its amino-terminal tyrosines
- The sulfate group at tyrosine 21 contributes substantially to the ability of CXCR4 to bind its ligand, stromal derived factor 1 1 alpha
- Tyrosine sulfation plays a less significant role in CXCR4-dependent HIV-1 entry than in CCR5-dependent HIV-1 entry
- In some cell lines, CXCR4 is efficiently modified by a chondroitin sulfate chain at serine 18 , but neither HIV-1 entry nor stromal derived factor 1 1 alpha binding was affected by loss of this glycosaminoglycan
- These data demonstrate a functional role for tyrosine sulfate in the CXC-chemokine receptor family and underscore a general difference in HIV-1 utilization of CCR5 and CXCR4
Output (sent_index, trigger,
protein,
sugar,
site):
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):