The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Role of Acetylation and Extracellular Location of Heat Shock Protein 90α in Tumor Cell Invasion
Open accessAbstract
Heat shock protein (hsp) 90 is an ATP-dependent molecular chaperone that maintains the active conformation of client oncoproteins in cancer cells. An isoform, hsp90α, promotes extracellular maturation of matrix metalloproteinase (MMP)-2, involved in tumor invasion and metastasis. Knockdown of histone deacetylase (HDAC) 6, which deacetylates lysine residues in hsp90, induces reversible hyperacetylation and attenuates ATP binding and chaperone function of hsp90. Here, using mass spectrometry, we identified seven lysine residues in hsp90α that are hyperacetylated after treatment of eukaryotic cells with a pan-HDAC inhibitor that also inhibits HDAC6. Depending on the specific lysine residue in the middle domain involved, although acetylation affects ATP, cochaperone, and client protein binding to hsp90α, acetylation of all seven lysines increased the binding of hsp90α to 17-allyl-amino-demethoxy geldanamycin. Notably, after treatment with the pan-HDAC inhibitor panobinostat (LBH589), the extracellular hsp90α was hyperacetylated and it bound to MMP-2, which was associated with increased in vitro tumor cell invasiveness. Treatment with antiacetylated hsp90α antibody inhibited in vitro invasion by tumor cells. Thus, reversible hyperacetylation modulates the intracellular and extracellular chaperone function of hsp90, and targeting extracellular hyperacetylated hsp90α may undermine tumor invasion and metastasis. [Cancer Res 2008;68(12):4833–42]
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Citations
Cites
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
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
Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
Ali, M. M. U., Roe, S. M., Vaughan, C. K., Meyer, P., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2006) · Nature · doi:10.1038/nature04716 · Cited by 962 · cited 1×
“These include the NH2-terminal nucleotide-binding domain, a middle domain (MD) that completes the ATPase site and binds to client proteins, as well as the COOH-terminal dimerization domain (7, 8).”
BackgroundZhao, R., Davey, M., Hsu, Y.-C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J., et al. (2005) · Cell · doi:10.1016/j.cell.2004.12.024 · Cited by 819
Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500186200 · Cited by 755
Self-citationMeyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00065-0 · Cited by 491
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 · cited 1×
“Although it is likely that not all of the known hsp90 client proteins would be uniformly affected (38), posttranslational modifications of hsp90 such as phosphorylation and acetylation influence the chaperone function of hsp90, thereby affecting the signaling networks that govern the malignant phenotype and response t…”
BackgroundMorishima, 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
Cited by
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498
Combining epigenetic drugs with other therapies for solid tumours — past lessons and future promise
Morel, D., Jeffery, D., Aspeslagh, S., Almouzni, G., & Postel-Vinay, S. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-019-0267-4 · Cited by 445
Regulation and function of the human HSP90AA1 gene
Zuehlke, A. D., Beebe, K., Neckers, L., & Prince, T. (2015) · Gene · doi:10.1016/j.gene.2015.06.018 · Cited by 347
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
Qian, C., Lai, C.-J., Bao, R., Wang, D.-G., Wang, J., Xu, G.-X., Atoyan, R., Qu, H., Yin, L., Samson, M., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-0055 · Cited by 248
Metadata
- Authors
- Yang, Y., Rao, R., Shen, J., Tang, Y., Fiskus, W., Nechtman, J., Atadja, P., & Bhalla, K.
- Venue
- Cancer Research
- Published
- 2008-06-15
- Volume
- 68
- Issue
- 12
- Pages
- 4833-4842
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- OpenAlex
- W2101096602
- Cited by
- 221
- References
- 9
- FWCI
- 7.32
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Yang, Y., Rao, R., Shen, J., Tang, Y., Fiskus, W., Nechtman, J., Atadja, P., & Bhalla, K. (2008). Role of Acetylation and Extracellular Location of Heat Shock Protein 90α in Tumor Cell Invasion. Cancer Research. https://doi.org/10.1158/0008-5472.can-08-0644
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