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Department of Internal Medicine, Division of Allergy and Immunology, University of Texas Medical Branch, Galveston, TX 77555
It has been shown that a membrane-proximal region within common ß
(ßc) receptor of IL-3/granulocyte-macrophage CSF/IL-5 (amino acids
450–517) is important for Lyn binding. We have shown previously that
Lyn kinase is physically associated with the IL-5R ßc subunit in
unstimulated cells. The result suggests that this association involves
binding modules that are not activation or phosphorylation dependent.
The objective of this study was to map the exact Lyn binding site on
ßc. Using overlapping and/or sequential peptides derived from ßc
450–517, we narrowed down the Lyn binding site to nine amino acid
residues, ßc 457–465. The P
A mutation in this region abrogated
the binding to Lyn, indicating a critical role of proline residues. We
created a cell-permeable Lyn-binding peptide by
N-stearation. This cell-permeable peptide blocked the
association of Lyn, but not Jak2 with ßc in situ. We also
investigated the ßc binding site of Lyn kinase. Our results suggest
that the N-terminal unique domain of Lyn kinase is important for
binding to ßc receptor. To our knowledge, this is the first molecular
identification of the Lyn binding site of ßc receptor. This finding
may help develop specific inhibitors of Lyn-coupled signaling
pathways.
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