Chaperone activity of αB-crystallin suppresses tubulin aggregation through complex formation

Cell Structure and Function

Volumn 22, Issue 5, 1997, Pages 539-544

  Arai, Hideaki ^a   Atomi, Yoriko ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Crystallin; HSP; Molecular chaperone; Tubulin

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; TUBULIN;

ARTICLE; CELL LYSATE; CENTRIFUGATION; COMPLEX FORMATION; DIMERIZATION; IMMUNOPRECIPITATION; MYOBLAST; PRIORITY JOURNAL; SUCROSE GRADIENT;

EID: 0031457379     PISSN: 03867196     EISSN: None     Source Type: Journal    
DOI: 10.1247/csf.22.539     Document Type: Article

References (33)

1. ARRIGO, A.-P. and LANDRY, J. 1994. Expression and function of low-molecular-weight heat shock proteins. In The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R.I., Tissieres, A., and Georgopoulos, C., eds.). Cold Spring Harbor Laboratory Press, New York, pp.335-373.
2. ATOMI, Y., YAMADA, S., and HONG, Y.-M. 1990. Dynamic expression of αB-crystallin in skeletal muscle Effects of unweighting, passive stretch and denervation. Proc. Japan Acad., 66 Ser B: 203-208.
3. ATOMI, Y., YAMADA, S., and NISHIDA, T. 1991. Early changes of αB-crystallin mRNA in rat skeletal muscle to mechanical tension and denervation. Biochem. Biophys. Res. Commun., 181: 1323-1330.
4. ATOMI, Y., YAMADA, S., STROHMAN, R., and NONOMURA, Y. 1991. αB-crystallin in skeletal muscle: purification and localization. J. Biochem., 110: 812-822.
5. BHAT, S.P. and NAGINENI, C.N. 1989. αB subunit of lens-specific protein alpha crystallin is present in other ocular and non-ocular tissues. Biochem. Biophys. Res. Commun., 158: 319-325.
6. DAS, K.P., PETRASH, J.M., and SUREWICZ, W.K. 1996. Conformational properties of substrate proteins bound to a molecular chaperone α-crystallin. J. Biol. Chem., 271: 10449-10452.
7. DEJONG, W.W., ZWEERS, A., VERSTEEG, M., and NUY-TERWINDT, E.C. 1984. Primary structures of the alpha-crystallin A chains of twenty-eight mammalian species, chicken and frog. Eur. J. Biochem., 141: 131-140.
8. DUBIN, R.A., WAWROUSEK, E.F., and PIATIGORSKY, J. 1989. Expression of the murine alpha B crystallin gene is not restricted to the lens. Mol. Cell. Biol., 9: 1083-1091.
9. FRYDMAN, J. and HARTL, F.U. 1994. Molecular chaperone functions of hsp70 and hsp60 in protein folding. In The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R.I., Tissieres, A., and Georgopoulos, C., eds.). Cold Spring Harbor Laboratory Press, New York, pp.251-284.
10. HIGHTOWER, L.E., SADIS, S.E., and TAKENAKA, I.M. 1994. Interactions of vertebrate hsc70 and hsp70 with unfolded proteins and peptides. In The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R.I., Tissieres, A., and Georgopoulos, C., eds.). Cold Spring Harbor Laboratory Press, New York, pp. 179-208.
11. HORWITZ, J. 1992. α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA, 89: 10449-10453.
12. INGOLIA, T.D. and CRAIG, E.A. 1982. Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin. Proc. Natl. Acad. Sci. USA, 79: 2360-2364.
13. IWAKI, T., IWAKI, A., TATEISHI, J., and GOLDMAN, J.E. 1994. Sense and antisense modification of glial αB-crystallin production results in alterations of stress fiber formation and thermoresistance. J. Cell Biol., 125: 1385-1393.
14. IWAKI, T., KUME-IWAKI, A., LIEM, R.K.H., and GOLDMAN, J.E. 1989. αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell, 57: 71-78.
15. JAKOB, U., GAESTEL, M., ENGEL, K., and BUCHNER, J. 1993. Small heat shock proteins are molecular chaperones. J. Biol. Chem., 268: 1517-1520.
16. KATO, K., ITO, H., INAGUMA, Y., OKAMOTO, K., and SAGA, S. 1996. Synthesis and accumulation of αB crystallin in C6 glioma cells is induced by agents that promote the disassembly of microtubules. J. Biol. Chem., 271: 26989-26994.
17. KLEMENZ, R., ANDRES, A.-C., FROHLI, E., SCHAFER, R., and AOYAMA, A. 1993. Expression of the murine small heat shock proteins hsp25 and alpha B crystallin in the absence of stress. J. Cell Biol., 120: 639-645.
18. KLEMENZ, R., FROHLI, E., AOYMAA, A., HOFFMANN, S., SIMPSON, R.J., MORITZ, R.L., and SCHAFER, R. 1991. Alpha B crystallin accumulation is a specific response to Ha-ras and v-mos oncogene expression in mouse NIH 3T3 fibroblasts. Mol. Cell. Biol., 11: 803-812.
19. KLEMENZ, R., FROHLI, E., STEIGER, R.H., SCHAFER, R., and AOYAMA, A. 1991. αB-Crystallin is a small heat shock protein. Proc. Natl. Acad. Sci. USA, 88: 3652-3656.
20. LEWIS, V.A., HYNES, G.M., ZHENG, D., SAIBIL, H., and WILLISON, K. 1992. T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Nature, 358: 249-252.
21. LINDQUIST, S. 1981. Regulation of protein synthesis during heat shock. Nature, 293: 311-314.
22. LINDQUIST, S. 1986. The heat-shock response. Annu. Rev. Biochem., 55: 1151-1191.
23. MERCK, K.B., GROENEN, P.J.T.A., VOORTER, C.E.M., DE HAARD-HOEKMAN, W.A., HORWITZ, J., BLOEMENDAL, H., and DE JONG, W.W. 1993. Structural and functional similarities of bovine α-crystallin and mouse small heat-shock protein. J. Biol. Chem., 268: 1046-1052.
24. NICHOLL, I.D. and QUINLAN, R.A. 1994. Chaperone activity of α-crystallins modulates intermediate filaments assembly. EMBO J., 13: 945-953.
25. PATERSON, Y. 1987. In Current Protocol in Molecular Biology (Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K., eds.). Green Publishing Associates Inc. and John Wiley and Sons, Inc., pp.11.15.1-4.
26. PRAKASH, V. and TIMASHEFF, S.N. 1982. Aging of tubulin at neutral pH. J. Mol. Biol., 160: 499-515.
27. PRASAD, A.R.S., LUDUENA, R.F., and HOROWITZ, P.M. 1986. Bis(8-anilinonaphthalene-1-sulfonate) as a probe for tubulin decay. Biochemistry, 25: 739-742.
28. RAMAN, B. and RAO, C.M. 1994. Chaperone-like activity and quarternary structure of α-crystallin. J. Biol. Chem., 269: 27264-27268.
29. RENKAWEK, K., DE JONG, W.W., MERCK, K.B., FRENKEN, C.W.G.M., and VAN WORKUM, F.P.A. 1992. αB-crystallin is present in reactive glia in Creutzfeldt-Jakob disease. Acta Neuropathologica, 83: 324-327.
30. RENKAWEK, K., VOORTER, C.E., BOSMAN, G.J., VAN WORKUM, P.P., and DE JONG, W.W. 1994. Expression of αB-crystallin in Alzheimer's disease. Acta Neuropathologica, 87: 155-160.
31. SHELANSKI, M.L., GASKIN, F., and CANTOR, C.R. 1973. Microtubule assembly in the absence of added nucleotides. Proc. Natl. Acad. Sci. USA, 70: 765-768.
32. WANG, K. and SPECTOR, A. 1994. The chaperone activity of bovine α crystallin Interaction with other lens crystallins in native and denatured states. J. Biol. Chem., 269: 13601-13608.
33. YAFFE, M.B., FARR, G.W., MIKLOS, D., HORWICH, A.L., STERNLICHT, M.L., and STERNLICHT, H. 1992. TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature, 358: 245-248.