Spectrin-Actin Interactions

  • Greg B. Ralston
Part of the Blood Cell Biochemistry book series (BLBI, volume 1)


The protein spectrin was first reported in 1968 in water-soluble extracts from erythrocyte membranes (Marchesi and Steers, 1968). Although for some time it was believed that spectrin represented a specific erythrocyte adaptation, in recent years spectrin and spectrinlike proteins have been found in a wide range of other cell types (e.g., see Goodman et al., 1981). These nonerythroid forms of spectrin all share with erythrocyte spectrin a common set of properties: they are proteins of high molecular mass, comprising two distinct subunits of approximately 250,000 and 230,000 Da, respectively; they bind calmodulin in a calcium-dependent manner, though with greatly differing affinities; they bind to actin filaments; and they are associated with the cell membranes through interaction with other proteins, particularly ankyrin (Bennett, 1985). Certainly in the red blood cell, and probably in other cell types, the major functional role of spectrin is to stabilize the membrane, and to provide a linkage for actin filaments to the membrane. While the red cell may be an inadequate model for other cell types, the organization of the erythrocyte cytoskeleton and its role in maintaining erythrocyte shape and deformability are now reasonably well understood, at least in broad terms, and the findings from the red cell give at least an indication of the organization of such molecules in other cells. The present discussion will be limited to erythrocyte spectrin.


Actin Filament Erythrocyte Membrane Human Erythrocyte Hereditary Spherocytosis Membrane Skeleton 
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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Greg B. Ralston
    • 1
  1. 1.Department of BiochemistryUniversity of SydneySydneyAustralia

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