Properties of brain spectrin (fodrin)

FEBS Letters

Ohanian, V.¹  Gratzer, W.B.¹  Burns, N.R.¹ 

[1] Medical Research Council Cell Biophysics Unit, King's College, Drury Lane, London WC 2B 5RL, England

关键词: Spectrin;    Fodrin;    Cytoskeleton;    Actin-binding protein;    Membrane;   

DOI  :  10.1016/0014-5793(83)80140-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Fodrin, a protein from bovine brain, immunologically related to spectrin, is shown, unlike some other proteins of generally similar appearance in the electron microscope, to resemble spectrin closely in its most distinctive structural characteristic, the very high α-helix content. Like spectrin, it is also insoluble below pH 5. One of the subunits only is phosphorylated by the cAMP-independent red cell membrane kinase, that phosphorylates the smaller subunit of spectrin. Fodrin also forms a ternary complex with F-actin and the third constituent of the red cell membranes cytoskeleton, protein 4.1. In the presence of 4.1 the interaction between fodrin and F-actin is enhanced. It is surmised that fodrin plays an analogous functional role in neuronal cells to that of spectrin in the red cell.

【 授权许可】

Unknown