Skip to main content

CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion.

Publication ,  Journal Article
Fong, AM; Alam, SM; Imai, T; Haribabu, B; Patel, DD
Published in: J Biol Chem
May 31, 2002

Fractalkine is a unique CX(3)C chemokine/mucin hybrid molecule that functions like selectins in inducing the capture of receptor-expressing cells. Because of the importance of tyrosine sulfation for ligand binding of the selectin ligand PSGL1, we tested the role of tyrosine sulfation for CX(3)CR1 function in cell adhesion. Tyrosine residues 14 and 22 in the N terminus of CX(3)CR1 were mutated to phenylalanine and stably expressed on K562 cells. Cells expressing CX(3)CR1-Y14F were competent in signal transduction but defective in capture by and firm adhesion to immobilized fractalkine under physiologic flow conditions. In static binding assays, CX(3)CR1-Y14F mutants had a 2-4-fold decreased affinity to fractalkine compared with wild type CX(3)CR1. By surface plasmon resonance measurements of fractalkine binding to biosensor chip-immobilized cell membranes, CX(3)CR1-Y14F mutants had a 100-fold decreased affinity to fractalkine. CX(3)CR1-expressing cell membranes treated with arylsulfatase to desulfate tyrosine residues also showed a 100-fold decreased affinity for fractalkine. Finally, synthesized, sulfated N-terminal CX(3)CR1 peptides immobilized on biosensor chips showed a higher affinity for fractalkine than non-sulfated peptides. Thus, we conclude that sulfation of tyrosine 14 enhances the function of CX(3)CR1 in cell capture and firm adhesion. Further, tyrosine sulfation may represent a general mechanism utilized by molecules that function in the rapid capture of circulating leukocytes.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

May 31, 2002

Volume

277

Issue

22

Start / End Page

19418 / 19423

Location

United States

Related Subject Headings

  • Tyrosine
  • Transfection
  • Time Factors
  • Surface Plasmon Resonance
  • Signal Transduction
  • Sequence Homology, Amino Acid
  • Receptors, HIV
  • Receptors, Cytokine
  • Phenylalanine
  • Mutation
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Fong, A. M., Alam, S. M., Imai, T., Haribabu, B., & Patel, D. D. (2002). CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion. J Biol Chem, 277(22), 19418–19423. https://doi.org/10.1074/jbc.M201396200
Fong, Alan M., S Munir Alam, Toshio Imai, Bodduluri Haribabu, and Dhavalkumar D. Patel. “CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion.J Biol Chem 277, no. 22 (May 31, 2002): 19418–23. https://doi.org/10.1074/jbc.M201396200.
Fong AM, Alam SM, Imai T, Haribabu B, Patel DD. CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion. J Biol Chem. 2002 May 31;277(22):19418–23.
Fong, Alan M., et al. “CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion.J Biol Chem, vol. 277, no. 22, May 2002, pp. 19418–23. Pubmed, doi:10.1074/jbc.M201396200.
Fong AM, Alam SM, Imai T, Haribabu B, Patel DD. CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion. J Biol Chem. 2002 May 31;277(22):19418–19423.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

May 31, 2002

Volume

277

Issue

22

Start / End Page

19418 / 19423

Location

United States

Related Subject Headings

  • Tyrosine
  • Transfection
  • Time Factors
  • Surface Plasmon Resonance
  • Signal Transduction
  • Sequence Homology, Amino Acid
  • Receptors, HIV
  • Receptors, Cytokine
  • Phenylalanine
  • Mutation