The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
The regulatory mechanism of Hsp90α secretion and its function in tumor malignancy
Open accessAbstract
Heat shock protein 90-α (Hsp90α) is an intracellular molecular chaperone. However, it can also be secreted with the underlying regulatory mechanism remaining far from clear. Here we show that the secreted Hsp90α is a C-terminal truncated form and its secretion is regulated by the C-terminal EEVD motif via interacting with proteins containing tetratricopeptide repeat domains. We also demonstrate that secretion of Hsp90α is determined by the phosphorylation status at residue Thr-90, regulated by protein kinase A and protein phosphatase 5. We further demonstrate that the secretion of Hsp90α is a prerequisite for its proinvasiveness function and blocking the secreted Hsp90α results in significant inhibition of tumor metastasis. Meanwhile, the level of plasma Hsp90α is positively correlated with tumor malignancy in clinical cancer patients. In sum, our results reveal the regulatory mechanism of Hsp90α secretion, and its function in tumor invasiveness, indicating it can be a promising diagnostic marker for tumor malignancy in clinical application.
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Cites
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches
McClellan, A. J., Xia, Y., Deutschbauer, A. M., Davis, R. W., Gerstein, M., & Frydman, J. (2007) · Cell · doi:10.1016/j.cell.2007.07.036 · Cited by 474
Structure and in vivo function of Hsp90
Pearl, L. H., & Prodromou, C. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00047-0 · Cited by 317
Russell, L. C., Whitt, S. R., Chen, M.-S., & Chinkers, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20060 · Cited by 165 · cited 1×
“S3) (21), showed no inhibitory effect (Fig.”
Cited by
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
High expression of small GTPase Rab3D promotes cancer progression and metastasis
Yang, J., Liu, W., Lu, X., Fu, Y., Li, L., & Luo, Y. (2015) · Oncotarget · doi:10.18632/oncotarget.3575 · Cited by 107
Self-citationPrognostic value of the mRNA expression of members of the HSP90 family in non‑small cell lung cancer
Liu, K., Kang, M., Li, J., Qin, W., & Wang, R. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.7228 · Cited by 47
Metadata
- Authors
- Wang, X., Song, X., Zhuo, W., Fu, Y., Shi, H., Liang, Y., Tong, M., Chang, G., & Luo, Y.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-12-15
- Volume
- 106
- Issue
- 50
- Pages
- 21288-21293
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1989480741
- Cited by
- 259
- References
- 4
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- green
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- Wang, X., Song, X., Zhuo, W., Fu, Y., Shi, H., Liang, Y., Tong, M., Chang, G., & Luo, Y. (2009). The regulatory mechanism of Hsp90α secretion and its function in tumor malignancy. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0908151106
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