Abstract
Spectrin and ankyrin are major components of a plasma membrane‐associated scaffold known as the spectrin cytoskeleton. Spectrin is thought to cross‐link actin filaments in a two‐dimensional submembrane network and ankyrin links the network to a number of integral membrane activities, including the sodium pump, voltage‐dependent sodium channels, and L1‐family cell adhesion molecules. Genetic studies have established that the spectrin cytoskeleton is required for the normal accumulation of these integral proteins at their normal sites of function. Defects in spectrin and ankyrin have been implicated in human disease, and studies in model genetic organisms are making it possible to elucidate the mechanisms behind their effects. Cell culture studies have also shed new light on the processes that govern formation of polarized membrane domains. This chapter surveys the results and their implications for the assembly and function of the spectrin cytoskeleton.
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