The binding of a ciliary microtubule plus-end binding protein complex to microtubules is regulated by ciliary protein kinase and phosphatase activities.
作者： R. H. Himes , W. L. Dentler , Wen Wang
DOI: 10.1016/S0021-9258(17)31826-4
关键词:
摘要: Using a human autoimmune CREST antiserum, we identified 97-kDa polypeptide at the plus ends of Tetrahymena ciliary microtubules and an antigen associated with mammalian kinetochores (Miller, J.M., Wang, W., Balczon, R., Dentler, W.L. (1990) J. Cell. Biol. 110, 703-714). The protein is part 1,500-2,000-kDa complex that can be released from in vitro assembled brain ATP gamma S (Wang, Suprenant, K.A., W. L. (1993) Chem. 268, 24796-24807). Here show ATP-dependent release inhibited, concentration-dependent manner, by calf intestine phosphatase kinase inhibitor 6-dimethylaminopurine. Sodium orthovanadate, phosphotyrosine inhibitor, stimulated microtubules. Therefore, fraction contains both activities, selective inhibition these activities necessary for binding When incubated [gamma-32P]ATP, portion phosphorylated as are several other polypeptides it. sensitivity requires low molecular weight heat-stable factor axonemes. These results suggest association regulated phosphorylation axoneme-associated kinases phosphatases.
sci-hub.st 参考文章(43)
G Wiche, High-Mr microtubule-associated proteins: properties and functions. Biochemical Journal. ,vol. 259, pp. 1- 12 ,(1989) , 10.1042/BJ2590001
W Chao, H Liu, D J Hanahan, M S Olson, Protein tyrosine phosphorylation and regulation of the receptor for platelet-activating factor in rat Kupffer cells. Effect of sodium vanadate. Biochemical Journal. ,vol. 288, pp. 777- 784 ,(1992) , 10.1042/BJ2880777
Julius A. Gordon, Use of vanadate as protein-phosphotyrosine phosphatase inhibitor. Methods in Enzymology. ,vol. 201, pp. 477- 482 ,(1991) , 10.1016/0076-6879(91)01043-2
W Wang, K Suprenant, W L Dentler, Reversible association of a 97-kDa protein complex found at the tips of ciliary microtubules with in vitro assembled microtubules. Journal of Biological Chemistry. ,vol. 268, pp. 24796- 24807 ,(1993) , 10.1016/S0021-9258(19)74535-9
L. Misconi, S. M. Van Patten, Heung-Chin Cheng, B. E. Kemp, R. B. Pearson, D. A. Walsh, A. J. Smith, A potent synthetic peptide inhibitor of the cAMP-dependent protein kinase. Journal of Biological Chemistry. ,vol. 261, pp. 989- 992 ,(1986) , 10.1016/S0021-9258(17)36041-6
T Kadowaki, Y Fujita-Yamaguchi, E Nishida, F Takaku, T Akiyama, S Kathuria, Y Akanuma, M Kasuga, Phosphorylation of tubulin and microtubule-associated proteins by the purified insulin receptor kinase. Journal of Biological Chemistry. ,vol. 260, pp. 4016- 4020 ,(1985) , 10.1016/S0021-9258(18)89224-9
J R Goldenring, B Gonzalez, J S McGuire, R J DeLorenzo, Purification and characterization of a calmodulin-dependent kinase from rat brain cytosol able to phosphorylate tubulin and microtubule-associated proteins. Journal of Biological Chemistry. ,vol. 258, pp. 12632- 12640 ,(1983) , 10.1016/S0021-9258(17)44223-2
F Wandosell, L Serrano, M A Hernández, J Avila, Phosphorylation of tubulin by a calmodulin-dependent protein kinase. Journal of Biological Chemistry. ,vol. 261, pp. 10332- 10339 ,(1986) , 10.1016/S0021-9258(18)67528-3
B. Zheng, C.F. Woo, J.F. Kuo, Mitotic arrest and enhanced nuclear protein phosphorylation in human leukemia K562 cells by okadaic acid, a potent protein phosphatase inhibitor and tumor promoter. Journal of Biological Chemistry. ,vol. 266, pp. 10031- 10034 ,(1991) , 10.1016/S0021-9258(18)99180-5
Junko Hirano-Ohnishi, Yoshio Watanabe, Ca2+/Calmodulin-Dependent Phosphorylation of Ciliary β-Tubulin in Tetrahymena The Journal of Biochemistry. ,vol. 105, pp. 858- 860 ,(1989) , 10.1093/OXFORDJOURNALS.JBCHEM.A122766