2-color photobleaching experiments reveal distinct intracellular dynamics of two components of the Hsp90 complex

Experimental Cell Research

Volumn 312, Issue 19, 2006, Pages 3949-3958

  Picard, Didier ^a   Suslova, Elena ^a   Briand, Pierre André ^a  

^a UNIVERSITY OF GENEVA   (Switzerland)

Author keywords

Confocal microscopy; Geldanamycin; In vivo; Interaction; Kinetics; Molecular chaperone

Indexed keywords

CELL PROTEIN; CHAPERONE; ENHANCED GREEN FLUORESCENT PROTEIN; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HYBRID PROTEIN; MCHERRY PROTEIN; MUTANT PROTEIN; PROTEIN; PROTEIN P23; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DIFFUSION; FLUORESCENCE RECOVERY AFTER PHOTOBLEACHING; HUMAN; HUMAN CELL; INTERMETHOD COMPARISON; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; WILD TYPE;

EID: 33750417953     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2006.08.026     Document Type: Article

References (48)

1. Giepmans B.N., Adams S.R., Ellisman M.H., and Tsien R.Y. The fluorescent toolbox for assessing protein location and function. Science 312 (2006) 217-224
2. Lippincott-Schwartz J., and Patterson G.H. Development and use of fluorescent protein markers in living cells. Science 300 (2003) 87-91
3. Sprague B.L., and McNally J.G. FRAP analysis of binding: proper and fitting. Trends Cell Biol. 15 (2005) 84-91
4. Sprague B.L., Pego R.L., Stavreva D.A., and McNally J.G. Analysis of binding reactions by fluorescence recovery after photobleaching. Biophys. J. 86 (2004) 3473-3495
5. Day R.N., and Schaufele F. Imaging molecular interactions in living cells. Mol. Endocrinol. 19 (2005) 1675-1686
6. Picard D. Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 59 (2002) 1640-1648
7. Whitesell L., and Lindquist S.L. HSP90 and the chaperoning of cancer. Nat. Rev., Cancer 5 (2005) 761-772
8. Pearl L.H., and Prodromou C. Structure and mechanism of the hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75 (2006) 271-294
9. Nathan D.F., Vos M.H., and Lindquist S. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 12949-12956
10. Caplan A.J. What is a co-chaperone?. Cell Stress Chaperones 8 (2003) 105-107
11. Picard D. Chaperoning steroid hormone action. Trends Endocrinol. Metab. 17 (2006) 229-235
12. Picard D. Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90. Exp. Cell Res. 312 (2006) 198-204
13. Johnson J.L., Beito T.G., Krco C.J., and Toft D.O. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol. Cell. Biol. 14 (1994) 1956-1963
14. Felts S.J., and Toft D.O. p23, a simple protein with complex activities. Cell Stress Chaperones 8 (2003) 108-113
15. Johnson J., Corbisier R., Stensgard B., and Toft D.O. The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes. J. Steroid Biochem. Mol. Biol. 56 (1996) 31-37
16. Johnson J.L., and Toft D.O. Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol. Endocrinol. 9 (1995) 670-678
17. Weaver A.J., Sullivan W.P., Felts S.J., Owen B.A., and Toft D.O. Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J. Biol. Chem. 275 (2000) 23045-23052
18. Prodromou C., Panaretou B., Chohan S., Siligardi G., O'Brien R., Ladbury J.E., Roe S.M., Piper P.W., and Pearl L.H. The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. EMBO J. 19 (2000) 4383-4392
19. Richter K., Walter S., and Buchner J. The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J. Mol. Biol. 342 (2004) 1403-1413
20. Siligardi G., Hu B., Panaretou B., Piper P.W., Pearl L.H., and Prodromou C. Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J. Biol. Chem. 279 (2004) 51989-51998
21. Sullivan W.P., Owen B.A., and Toft D.O. The influence of ATP and p23 on the conformation of hsp90. J. Biol. Chem. 277 (2002) 45942-45948
22. McLaughlin S.H., Smith H.W., and Jackson S.E. Stimulation of the weak ATPase activity of human Hsp90 by a client protein. J. Mol. Biol. 315 (2002) 787-798
23. Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., Prodromou C., and Pearl L.H. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440 (2006) 1013-1017
24. Neckers L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol. Med. 8 (2002) S55-S61
25. Isaacs J.S., Xu W., and Neckers L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 3 (2003) 213-217
26. Workman P. Overview: translating Hsp90 biology into Hsp90 drugs. Curr. Cancer Drug Targets 3 (2003) 297-300
27. Shaner N.C., Campbell R.E., Steinbach P.A., Giepmans B.N., Palmer A.E., and Tsien R.Y. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22 (2004) 1567-1572
28. Song H.Y., Dunbar J.D., Zhang Y.X., Guo D.Q., and Donner D.B. Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 270 (1995) 3574-3581
29. Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67 (1998) 509-544
30. Felts S.J., Owen B.A., Nguyen P., Trepel J., Donner D.B., and Toft D.O. The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J. Biol. Chem. 275 (2000) 3305-3312
31. van Bergen en Henegouwen P.M., Berbers G., Linnemans W.A., and van Wijk R. Subcellular localization of the 84,000 dalton heat-shock protein in mouse neuroblastoma cells: evidence for a cytoplasmic and nuclear location. Eur.J. Cell Biol. 43 (1987) 469-478
32. Berbers G.A., Kunnen R., van Bergen en Henegouwen P.M., and van Wijk R. Localization and quantitation of hsp84 in mammalian cells. Exp. Cell Res. 177 (1988) 257-271
33. Akner G., Mossberg K., Sundqvist K.G., Gustafsson J.-Å., and Wikström A.C. Evidence for reversible, non-microtubule and non-microfilament-dependent nuclear translocation of hsp90 after heat shock in human fibroblasts. Eur.J. Cell Biol. 58 (1992) 356-364
34. Langer T., Rosmus S., and Fasold H. Intracellular localization of the 90 kDA heat shock protein (HSP90α) determined by expression of a EGFP-HSP90α-fusion protein in unstressed and heat stressed 3T3 cells. Cell Biol. Int. 27 (2003) 47-52
35. Soumpasis D.M. Theoretical analysis of fluorescence photobleaching recovery experiments. Biophys. J. 41 (1983) 95-97
36. Stenoien D.L., Nye A.C., Mancini M.G., Patel K., Dutertre M., O'Malley B.W., Smith C.L., Belmont A.S., and Mancini M.A. Ligand-mediated assembly and real-time cellular dynamics of estrogen receptor α-coactivator complexes in living cells. Mol. Cell. Biol. 21 (2001) 4404-4412
37. Zimmermann T. Spectral imaging and linear unmixing in light microscopy. Adv. Biochem. Eng. Biotechnol. 95 (2005) 245-265
38. Zimmermann T., Rietdorf J., and Pepperkok R. Spectral imaging and its applications in live cell microscopy. FEBS Lett. 546 (2003) 87-92
39. Scholz G.M., Cartledge K., and Hall N.E. Identification and characterization of Harc: a novel Hsp90 associating relative of Cdc37. J. Biol. Chem. 18 (2001) 18
40. Harst A., Lin H., and Obermann W.M. Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation. Biochem. J. 387 (2005) 789-796
41. Pratt W.B., and Toft D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev. 18 (1997) 306-360
42. Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W., and Pearl L.H. Structural basis for inhibition of the hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42 (1999) 260-266
43. Dittmar K.D., Hutchison K.A., Owens-Grillo J.K., and Pratt W.B. Reconstitution of the steroid receptor ̇hsp90 heterocomplex assembly system of rabbit reticulocyte lysate. J. Biol. Chem. 271 (1996) 12833-12839
44. Chen S., Prapapanich V., Rimerman R.A., Honoré B., and Smith D.F. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins Hsp90 and Hsp70. Mol. Endocrinol. 10 (1996) 682-693
45. Johnson B.D., Schumacher R.J., Ross E.D., and Toft D.O. Hop modulates hsp70/hsp90 interactions in protein folding. J. Biol. Chem. 273 (1998) 3679-3686
46. Odunuga O.O., Longshaw V.M., and Blatch G.L. Hop: more than an Hsp70/Hsp90 adaptor protein. BioEssays 26 (2004) 1058-1068
47. Smith D.F. Tetratricopeptide repeat cochaperones in steroid receptor complexes. Cell Stress Chaperones 9 (2004) 109-121
48. Smith D.F., Whitesell L., Nair S.C., Chen S., Prapapanich V., and Rimerman R.A. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol. 15 (1995) 6804-6812