Abstract
Spectrin, a member of the family of actin cross-linking proteins that also includes dystrophin and α-actinin, is a widely distributed protein in eukaryotes (Dubreuil 1991; Matsudaira 1991). Spectrin is generally thought to generate networks that support the plasma membrane and sustain interactions between cellular structures responsible for cell motility and shape, but this hypothesis concerning its function is derived largely from studies of the human erythrocyte. While it is clear that the membrane skeleton of erythrocytes is a spectrin network that contributes to cell shape (Branton et al. 1981; Elgsaeter et al. 1986; Marchesi 1985), cell shape in most nonerythroid cells is governed by an extensive transcellular cytoskeleton. Whether or not spectrin’s network-forming capacity is the basis for in vivo function in these nonerythroid systems has not been addressed.
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© 1995 Springer-Verlag Berlin Heidelberg
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Branton, D. (1995). Spectrin Interchain Binding in Drosophila Development. In: Jockusch, B.M., Mandelkow, E., Weber, K. (eds) The Cytoskeleton. Colloquium der Gesellschaft für Biologische Chemie 14.–16. April 1994 in Mosbach/Baden, vol 45. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79482-7_7
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DOI: https://doi.org/10.1007/978-3-642-79482-7_7
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