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aDepartment of Clinical and Experimental Pharmacology, University of Adelaide, Adelaide, Australia bDepartment of Biology, Jackson State University, Jackson, Mississippi 39216, USA
Address for correspondence: Ian F. Musgrave, Department of Clinical and Experimental Pharmacology, University of Adelaide, Adelaide 5005, Australia. Voice: (+61) 8 8303 3905; fax (+61) 8 8224 0685. e-mail: ian.musgrave{at}adelaide.edu.au Ann. N.Y. Acad. Sci. 1009: 413-418 (2003)
IRAS, a putative clone of the I1-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 b3-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.
Key Words: imidazoline receptors • signal transduction • integrin • scaffold • tyrosine kinase • Nischarin
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