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AJP - Cell Physiology, Vol 270, Issue 5 C1263-C1270, Copyright © 1996 by American Physiological Society
ARTICLES |
K. A. Beck and W. J. Nelson
Department of Molecular and Cellular Physiology, Stanford University School of Medicine, California 94305-5426, USA.
Normal cell function is dependent on the existence of membrane compartments that have unique populations of membrane proteins. Sorting of membrane proteins forms the basis for the biogenesis of distinct membrane compartments. There are many examples of membrane protein-sorting events in cells, but the molecular machinery involved is poorly understood. We discuss characteristics of a putative membrane protein-sorting machine and show that the spectrin-based membrane skeleton conforms to these characteristics. The spectrin-based membrane skeleton is a submembranous, spatially limited, two-dimensional lattice that binds a subset of membrane proteins. These properties allow the membrane skeleton to facilitate the formation of distinct membrane domains and thus reveal its potential as a membrane protein-sorting machine.
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