The neural cell spectrin skeleton: a review

Abstract

The discovery of nonerythroid spectrin (Goodman et al., Proc. Natl. Acad. Sci. USA 78: 7570-7574, 1981) has generated interest equivalent to that occurring upon the identification of nonmuscle actin and myosin. Brain spectrin has become the best-studied member of the nonerythroid spectrin family of molecules. In this review, we discuss the structure and functional interactions of brain spectrin, as a prelude to attempting to resolve what are some of the more controversial questions in the field. We finish with a discussion of what may be the most profitable directions for future research.

Hts, the Drosophila homologue of adducin, physically interacts with the transmembrane receptor golden goal to guide photoreceptor axons

“…Since the Actin-Spectrin cytoskeleton is supposed to organize integral membrane proteins (Goodman andZagon, 1984, 1986), we wondered whether a possible impairment of the ActinSpectrin cytoskeleton caused by the loss of Hts would lead to a change in the distribution of Gogo.…”

Synaptic plasticity in early aging

“…This surprising correspondence with the time course of LTP consolidation is suggestive of a causal relationship, in which some set of events stabilizes newly assembled actin filaments and thereby stabilizes the new spine morphologies they support. The most likely candidate for a consolidation process of this type is cross-linking of the actin filaments, a function executed by a handful of proteins, the most prominent of which is spectrin (Goodman and Zagon, 1986;Fox et al, 1987;Bennett and Lambert, 1991) and its homologues. Spectrin is concentrated in adult brain membranes (Siman et al, 1987) and theta burst stimulation, applied at threshold levels for inducing LTP, causes its proteolysis , evidently through activation of the calcium sensitive protease calpain (Bednarski et al, 1995;Vanderklish et al, 1995Vanderklish et al, , 1996.…”

Functional diversity among spectrin isoforms

“…The direct visualization of ankyrin [Davis and Bennett, 1984b], calmodulin [Tsukita et al, 19831, and antigenic sites [Glenney et al, 1983al on mammalian brain spectrin and the mapping of human brain spectrin functional domains [Harris and Morrow, 1988b;Harris et al, 19881 indicate that these tetramers are arranged in an erythroid-like head-to-head manner. Given the similar composition and morphology of other nonerythroid spectrins, it is likely that all spectrin tetramers are arranged in a similar Bennett [ 19851;3, Bloch and Morrow [1989]; 4, Branton et al [1981]; 5, Byers et al [ 19871;6 , Coleman et al [1989]; 7, Dubreuil et al [1987]; 8, Fishkind et al [1987]; 9, Giebelhaus et al 119871;10, Glenney and Glenney [1983a]; 11, ; 12, Glenney et al [1982b]; 13, ; 14, Goodman and Zagon [1986]; 15, Kuramochi et al [1986]; 16, Lazarides and Nelson [1985]; 17, Marchesi [1985]; 18, ; 19, Pearl et al [1984];20, Pollard 119841;21, Shatten et al [1986]; 22, Shile et al [1985]; 23, Repasky et al [1982]; 24, Riederer et al [1986].…”