Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin.

作者: R T Moon , A P McMahon

DOI: 10.1016/S0021-9258(19)39582-1

关键词:

摘要: Nonerythroid alpha-spectrin (alpha-fodrin) is a major component of the membrane skeleton in diverse cell types. Overlapping cDNAs have been isolated which encompass coding region human lung fibroblast nonerythroid alpha-spectrin. The composite sequence 7,787 nucleotides encodes polypeptide 2,472 amino acids (predicted Mr 283,964). This has 58% acid identity with erythroid alpha-spectrin, encoded on different gene, and 96% full-length chicken brain We previously reported variable expression 20 between repeats 10 11 (McMahon, A. P., Giebelhaus, D. H., Champion, J. E., Bailes, A., Lacey, S., Carritt, B., Henchman, S. K., Moon, R. T. (1987) Differentiation 34, 68-78). In this study, we report additional heterogeneity near carboxyl-terminal end. One (clone 3D) an in-frame deletion 18 within spectrin repeat 21 when compared to overlapping cDNA 7). As occurs domains suggested bind calcium or actin, it possible that fibroblasts express functionally distinct isoforms

参考文章(46)
J.P. Anderson, J.S. Morrow, The interaction of calmodulin with human erythrocyte spectrin. Inhibition of protein 4.1-stimulated actin binding. Journal of Biological Chemistry. ,vol. 262, pp. 6365- 6372 ,(1987) , 10.1016/S0021-9258(18)45579-2
K E Sahr, P Laurila, L Kotula, A L Scarpa, E Coupal, T L Leto, A J Linnenbach, J C Winkelmann, D W Speicher, V T Marchesi, The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin. Journal of Biological Chemistry. ,vol. 265, pp. 4434- 4443 ,(1990) , 10.1016/S0021-9258(19)39583-3
M D Baron, M D Davison, P Jones, D R Critchley, The sequence of chick alpha-actinin reveals homologies to spectrin and calmodulin. Journal of Biological Chemistry. ,vol. 262, pp. 17623- 17629 ,(1987) , 10.1016/S0021-9258(18)45426-9
A S Harris, D E Croall, J S Morrow, The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site. Journal of Biological Chemistry. ,vol. 263, pp. 15754- 15761 ,(1988) , 10.1016/S0021-9258(19)37652-5
W J Hong, D Doyle, Cloning and Analysis of cDNA clones for Rat Kidney α-Spectrin Journal of Biological Chemistry. ,vol. 264, pp. 12758- 12764 ,(1989) , 10.1016/S0021-9258(18)51550-7
Veli-Matti Wasenius, Matti Saraste, Petri Salven, Marja Erämaa, Liisa Holm, Veli-Pekka Lehto, Primary structure of the brain alpha-spectrin. Journal of Cell Biology. ,vol. 108, pp. 79- 93 ,(1989) , 10.1083/JCB.108.1.79
J. G. Conboy, J. Chan, N. Mohandas, Y. W. Kan, Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells Proceedings of the National Academy of Sciences of the United States of America. ,vol. 85, pp. 9062- 9065 ,(1988) , 10.1073/PNAS.85.23.9062
Matthew D. Davison, Michael D. Baron, David R. Critchley, John C. Wootton, Structural analysis of homologous repeated domains in α-actinin and spectrin International Journal of Biological Macromolecules. ,vol. 11, pp. 81- 90 ,(1989) , 10.1016/0141-8130(89)90047-0