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Minireview: Integral Membrane Proteins that Function Coordinately with the Insulin-Like Growth Factor I Receptor to Regulate Intracellular Signaling

Department of Endocrinology and Metabolism, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599

Address all correspondence and requests for reprints to: David R. Clemmons, M.D., 6111 Thurston Bowles, CB 7170, Department of Medicine, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599. E-mail: dpm{at}med.unc.edu.

Integral membrane proteins that are present on cell surfaces bind to extracellular ligands, and this binding influences multiple cellular processes. Three cell surface proteins, Vß3 integrin, integrin associated protein, and SHPS-1, have been shown to modulate both IGF-I receptor-linked signaling and cellular growth and migration responses that are stimulated by IGF-I. Ligand occupancy of these three proteins influences the recruitment of the phosphatase SHP-2 to the IGF-I receptor and thereby modulates the duration of IGF-I receptor tyrosine phosphorylation. In addition, changes in ligand occupancy of these three integral membrane proteins can regulate the transfer of SHP-2 phosphatase to downstream signaling molecules, which is also required for stimulation of cell migration and DNA synthesis by IGF-I. Determination of the spectrum of ligands for these three integral membrane proteins and the mechanisms by which each ligand functions to alter IGF-I signaling are important objectives of future research.

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