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Assembly of PRR‐Containing Receptors on Scaffolds: A Model for Imidazoline I1‐Receptor Action
Author(s) -
MUSGRAVE IF,
DEHLE FC,
PILETZ J
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1304.055
Subject(s) - receptor , signal transduction , receptor protein tyrosine kinases , microbiology and biotechnology , integrin , imidazoline receptor , chemistry , receptor tyrosine kinase , biology , biochemistry , pharmacology
A bstract : IRAS, a putative clone of the I 1 ‐imidazoline receptor, possesses a proline‐rich region (PRR) motif, which might interact with SH3 regions on tyrosine kinases, and an integrin‐binding motif. Receptors with a PRR motif can generally assemble onto multi‐element signaling complexes (eg., the b 3 ‐receptor on the EGF receptor) and thereby modulate signal transduction. Integrins serve as scaffolds for multi‐element signaling complexes, similar to that assembled with the EGF receptor. It is therefore possible that IRAS signals through a complex with other receptors.