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Published online
doi:10.1083/jcb.200811059
The Journal of Cell Biology, Vol. 185, No. 3, 381-385
The Rockefeller University Press, 0021-9525 $30.00
© Lajoie et al.
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Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane



Patrick Lajoie1, Jacky G. Goetz1, James W. Dennis2, and Ivan R. Nabi1

1 Deptartment of Cellular and Physiological Sciences, Life Sciences Institute University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada
2 Samuel Lunenfeld Research Institute, Toronto, Ontario M5G 1X5, Canada

Correspondence to Ivan R. Nabi: ivan.robert.nabi{at}ubc.ca

The plasma membrane is organized into various subdomains of clustered macromolecules. Such domains include adhesive structures (cellular synapses, substrate adhesions, and cell–cell junctions) and membrane invaginations (clathrin-coated pits and caveolae), as well as less well-defined domains such as lipid rafts and lectin-glycoprotein lattices. Domains are organized by specialized scaffold proteins including the intramembranous caveolins, which stabilize lipid raft domains, and the galectins, a family of animal lectins that cross-link glycoproteins forming molecular lattices. We review evidence that these heterogeneous microdomains interact to regulate substratum adhesion and cytokine receptor dynamics at the cell surface.

P. Lajoie and J.G. Goetz contributed equally to this paper.

P. Lajoie's present address is the Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, New York, NY 10461.

J.G. Goetz's present address is Department of Vascular Biology and Inflammation, Centro Nacional de Investigaciones Cardiovasculares, Madrid E-28029, Spain.

Abbreviations used in this paper: EGFR, epidermal growth factor receptor; GPI, glycosylphosphatidylinositol; STALL, stimulation-induced temporary arrest of lateral diffusion; TCR, T cell receptor.

© 2009 Lajoie et al.
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