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TRANSLOCATION OF THE IL‐1 RECEPTOR TO FOCAL ADHESIONS IS REGULATED THROUGH THE C‐TERMINAL END OF THE CYTOPLASMIC DOMAIN
Author(s) -
Huang WY.,
Vallés S.,
Qwarnstrom E. E.
Publication year - 2001
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.2000.0666
Subject(s) - focal adhesion , microbiology and biotechnology , receptor , fusion protein , chromosomal translocation , vinculin , biology , transmembrane protein , transmembrane domain , cytoplasm , 5 ht5a receptor , fibronectin , signal transduction , biochemistry , gene , extracellular matrix , recombinant dna
The mechanisms of translocation of the IL‐1 receptor to focal adhesions were analysed using EGFP reporter constructs and confocal microscopy. In fibronectin‐attached cells, the receptor fusion protein was present in distinct punctate areas, co‐localizing with the transmembrane‐linkage protein vinculin. In migrating cells, the two proteins co‐localized at the leading edge in ruffle‐like structures. Experiments using a series of receptor mutants revealed that translocation of the IL‐1 receptor to focal adhesions was dependent on motifs conserved between members of the TIR family, in the C‐terminal end of the receptor. Further, an enhanced level of expression of the wild‐type receptor at attachment sites was shown to correlate with an increased severity of IL‐1 induced structural effects. This report demonstrates that translocation of the IL‐1 receptor to focal adhesions is dependent on conserved domains in the C‐terminal end of the protein, and that receptor localization at these sites is important in structural regulation of IL‐1 mediated responses.