The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Regulation of the Dynamics of hsp90 Action on the Glucocorticoid Receptor by Acetylation/Deacetylation of the Chaperone
Open accessAbstract
It is known that inhibition of histone deacetylases (HDACs) leads to acetylation of the abundant protein chaperone hsp90. In a recent study, we have shown that knockdown of HDAC6 by a specific small interfering RNA leads to hyperacetylation of hsp90 and that the glucocorticoid receptor (GR), an established hsp90 "client" protein, is defective in ligand binding, nuclear translocation, and gene activation in HDAC6-deficient cells (Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., and Yao, T-P. (2005) Mol. Cell 18, 601-607). Using human embryonic kidney wild-type and HDAC6 (small interfering RNA) knockdown cells transiently expressing the mouse GR, we show here that the intrinsic properties of the receptor protein itself are not affected by HDAC6 knockdown, but the knockdown cytosol has a markedly decreased ability to assemble stable GR.hsp90 heterocomplexes and generate stable steroid binding activity under cell-free conditions. HDAC6 knockdown cytosol has the same ability to carry out dynamic GR.hsp90 heterocomplex assembly as wild-type cytosol. Addition of purified hsp90 to HDAC6 knockdown cytosol restores stable GR.hsp90 heterocomplex assembly to the level of wild-type cytosol. hsp90 from HDAC6 knockdown cytosol has decreased ATP-binding affinity, and it does not assemble stable GR.hsp90 heterocomplexes when it is a component of a purified five-protein assembly system. Incubation of knockdown cell hsp90 with purified HDAC6 converts the hsp90 to wild-type behavior. Thus, acetylation of hsp90 results in dynamic GR.hsp90 heterocomplex assembly/disassembly, and this is manifest in the cell as a approximately 100-fold shift to the right in the steroid dose response for gene activation.
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HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
Self-citationNuclear protein CBP is a coactivator for the transcription factor CREB
Kwok, R. P. S., Lundblad, J. R., Chrivia, J. C., Richards, J. P., Bächinger, H. P., Brennan, R. G., Roberts, S. G. E., Green, M. R., & Goodman, R. H. (1994) · Nature · doi:10.1038/370223a0 · Cited by 1,443
HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153
Self-citationModulation of p53, ErbB1, ErbB2, and Raf-1 Expression in Lung Cancer Cells by Depsipeptide FR901228
Yu, X. (2002) · CancerSpectrum Knowledge Environment · doi:10.1093/jnci/94.7.504 · Cited by 360
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
Pratt, W. B., Galigniana, M. D., Harrell, J. M., & DeFranco, D. B. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.02.004 · Cited by 285
Self-citationMorishima, Y., Murphy, P. J. M., Li, D.-P., Sanchez, E. R., & Pratt, W. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000434200 · Cited by 166
Self-citationHsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus
Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., & Pratt, W. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402223200 · Cited by 150
Evidence for glucocorticoid receptor transport on microtubules by dynein
Harrell, J. M., Murphy, P. J. M., Morishima, Y., Chen, H., Mansfield, J. F., Galigniana, M. D., & Pratt, W. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406863200 · Cited by 129
The Influence of ATP and p23 on the Conformation of hsp90
Sullivan, W. P., Owen, B. A. L., & Toft, D. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207754200 · Cited by 111
Morishima, Y., Kanelakis, K. C., Murphy, P. J. M., Lowe, E. R., Jenkins, G. J., Osawa, Y., Sunahara, R. K., & Pratt, W. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309814200 · Cited by 97
Self-citation
Cited by
An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function
Scroggins, B. T., Robzyk, K., Wang, D., Marcu, M. G., Tsutsumi, S., Beebe, K., Cotter, R. J., Felts, S., Toft, D., Karnitz, L., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.008 · Cited by 413
HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
Boyault, C., Sadoul, K., Pabion, M., & Khochbin, S. (2007) · Oncogene · doi:10.1038/sj.onc.1210614 · Cited by 397
Marzec, M., Eletto, D., & Argon, Y. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.10.013 · Cited by 390
Histone deacetylase 6 interacts with the microtubule‐associated protein tau
Ding, H., Dolan, P. J., & Johnson, G. V. W. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05564.x · Cited by 387
Post-translational modifications of Hsp90 and their contributions to chaperone regulation
Mollapour, M., & Neckers, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.018 · Cited by 288
Metadata
- Authors
- Murphy, P. J. M., Morishima, Y., Kovacs, J. J., Yao, T.-P., & Pratt, W. B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-10
- Volume
- 280
- Issue
- 40
- Pages
- 33792-33799
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2091973193
- Cited by
- 164
- References
- 10
- FWCI
- 5.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
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