BAG‐1 modulates the chaperone activity of Hsp70/Hsc70
作者： Shinichi Takayama , David N Bimston , Shu-ichi Matsuzawa , Brian C Freeman , Christine Aime-Sempe
关键词: Hsp33 、 Cell signaling 、 Biochemistry 、 Cell biology 、 Biology 、 Receptor 、 BAG domain 、 Chaperone (protein) 、 HSC70 Heat-Shock Proteins 、 Transcription factor 、 Plasma protein binding
摘要: The 70 kDa heat shock family of molecular chaperones is essential to a variety cellular processes, yet it unclear how these proteins are regulated in vivo. We present evidence that the protein BAG-1 potential modulator chaperones, Hsp70 and Hsc70. binds ATPase domain Hsc70, without requirement for their carboxy-terminal peptide-binding domain, can be co-immunoprecipitated with Hsp/Hsc70 from cell lysates. Purified efficiently form heteromeric complexes vitro. inhibits Hsp/Hsc70-mediated vitro refolding an unfolded substrate, whereas mutants fail bind do not affect chaperone activity. binding one its known targets, Bcl-2, lysates was found dependent on ATP, consistent possible involvement complex formation. Overexpression also protected certain lines shock-induced death. identification as partner may explain diverse interactions observed between several other proteins, including Raf-1, steroid hormone receptors tyrosine kinase growth factor receptors. inhibitory effects activity suggest represents novel type regulatory thus link signaling, death stress response.
core.ac.uk
nature.com
sci-hub.se 参考文章(40)
M. Wartmann, R.J. Davis, The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. Journal of Biological Chemistry. ,vol. 269, pp. 6695- 6701 ,(1994) , 10.1016/S0021-9258(17)37431-8
K.A. Hutchison, K.D. Dittmar, M.J. Czar, W.B. Pratt, Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90. Journal of Biological Chemistry. ,vol. 269, pp. 5043- 5049 ,(1994) , 10.1016/S0021-9258(17)37651-2
L.F. Stancato, Y.H. Chow, K.A. Hutchison, G.H. Perdew, R Jove, W.B. Pratt, Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system Journal of Biological Chemistry. ,vol. 268, pp. 21711- 21716 ,(1993) , 10.1016/S0021-9258(20)80600-0
A. Bardelli, P. Longati, D. Albero, S. Goruppi, C. Schneider, C. Ponzetto, P. M. Comoglio, HGF receptor associates with the anti-apoptotic protein BAG-1 and prevents cell death. The EMBO Journal. ,vol. 15, pp. 6205- 6212 ,(1996) , 10.1002/J.1460-2075.1996.TB01009.X
John C. Reed, Double identity for proteins of the Bcl-2 family Nature. ,vol. 387, pp. 773- 776 ,(1997) , 10.1038/42867
D S Latchman, Katz, J Galea-Lauri, A J Richardson, Increased Heat Shock Protein 90 (hsp90) Expression Leads to Increased Apoptosis in the Monoblastoid Cell Line U937 Following Induction With TNF-alpha and Cycloheximide: A Possible Role in Immunopathology Journal of Immunology. ,vol. 157, pp. 4109- 4118 ,(1996)
B. C. Freeman, R. I. Morimoto, The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. The EMBO Journal. ,vol. 15, pp. 2969- 2979 ,(1996) , 10.1002/J.1460-2075.1996.TB00660.X
Erica A. Golemis, Ilya Serebriiskii, Russell L. Finley, Mikhail G. Kolonin (hunt by interaction mating, Jeno Gyuris, Roger Brent, Interaction trap/two-hybrid system to identify interacting proteins. Current protocols in protein science. ,vol. 82, ,(1997) , 10.1002/0471140864.PS1902S57
L. G. Davis, W. M. Kuehl, J. F. Battey, Basic methods in molecular biology ,(1986)
Steven W. Muchmore, Michael Sattler, Heng Liang, Robert P. Meadows, John E. Harlan, Ho Sup Yoon, David Nettesheim, Brian S. Chang, Craig B. Thompson, Sui-Lam Wong, Shi-Chung Ng, Stephen W. Fesik, X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature. ,vol. 381, pp. 335- 341 ,(1996) , 10.1038/381335A0