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Am J Physiol Cell Physiol 288: C20-C29, 2005; doi:10.1152/ajpcell.00368.2004
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INVITED REVIEW

PDZ proteins retain and regulate membrane transporters in polarized epithelial cell membranes

Bert Brône and Jan Eggermont

Laboratory of Physiology, Katholieke Universiteit Leuven, Campus Gasthuisberg O & N, Leuven, Belgium

PDZ proteins retain and regulate membrane transporters in polarized epithelial cell membranes. Am J Physiol Cell Physiol 288: C20–C29, 2005; doi:10.1152/ajpcell.00368.2004.—The plasma membrane of epithelial cells is subdivided into two physically separated compartments known as the apical and basolateral membranes. To obtain directional transepithelial solute transport, membrane transporters (i.e., ion channels, cotransporters, exchangers, and ion pumps) need to be targeted selectively to either of these membrane domains. In addition, the transport properties of an epithelial cell will be maintained only if these membrane transporters are retained and properly regulated in their specific membrane compartments. Recent reports have indicated that PDZ domain-containing proteins play a dual role in these processes and, in addition, that different apical and basolateral PDZ proteins perform similar tasks in their respective membrane domains. First, although PDZ-based interactions are dispensable for the biosynthetic targeting to the proper membrane domain, the PDZ network ensures that the membrane proteins are efficiently retained at the cell surface. Second, the close spatial positioning of functionally related proteins (e.g., receptors, kinases, channels) into a signal transduction complex (transducisome) allows fast and efficient control of membrane transport processes.

retention of apical and basolateral membrane proteins; transducisomes; protein complex formation



Address for reprint requests and other correspondence: J. Eggermont, Laboratory of Physiology, Campus Gasthuisberg O & N, Catholic University of Leuven, Herestraat 49, B-3000 Leuven, Belgium (E-mail: Jan.Eggermont{at}med.kuleuven.ac.be)




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