The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress
Open accessAbstract
The efficient clearance of cytotoxic misfolded protein aggregates is critical for cell survival. Misfolded protein aggregates are transported and removed from the cytoplasm by dynein motors via the microtubule network to a novel organelle termed the aggresome where they are processed. However, the means by which dynein motors recognize misfolded protein cargo, and the cellular factors that regulate aggresome formation, remain unknown. We have discovered that HDAC6, a microtubule-associated deacetylase, is a component of the aggresome. We demonstrate that HDAC6 has the capacity to bind both polyubiquitinated misfolded proteins and dynein motors, thereby acting to recruit misfolded protein cargo to dynein motors for transport to aggresomes. Indeed, cells deficient in HDAC6 fail to clear misfolded protein aggregates from the cytoplasm, cannot form aggresomes properly, and are hypersensitive to the accumulation of misfolded proteins. These findings identify HDAC6 as a crucial player in the cellular management of misfolded protein-induced stress.
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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-citationAggresomes: A Cellular Response to Misfolded Proteins
Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148
HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., & Matthias, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg115 · Cited by 740
In vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation
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Seigneurin-Berny, D., Verdel, A., Curtet, S., Lemercier, C., Garin, J., Rousseaux, S., & Khochbin, S. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.8035-8044.2001 · Cited by 335
Histone deacetylases: transcriptional repression with SINers and NuRDs
Ayer, D. E. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01536-6 · Cited by 274
Molecular Cloning and Characterization of a Novel Histone Deacetylase HDAC10
Guardiola, A. R., & Yao, T.-P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109861200 · Cited by 253
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Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Anticancer activities of histone deacetylase inhibitors
Bolden, J. E., Peart, M. J., & Johnstone, R. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2133 · Cited by 2,919
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Xu, W. S., Parmigiani, R. B., & Marks, P. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210620 · Cited by 1,542
New and emerging HDAC inhibitors for cancer treatment
West, A. C., & Johnstone, R. W. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69738 · Cited by 1,404
HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.
Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234
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Metadata
- Authors
- Kawaguchi, Y., Kovacs, J. J., McLaurin, A., Vance, J. M., Ito, A., & Yao, T.-P.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2003-12
- Volume
- 115
- Issue
- 6
- Pages
- 727-738
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2090926709
- Cited by
- 1,524
- References
- 7
- FWCI
- 9.11
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Kawaguchi, Y., Kovacs, J. J., McLaurin, A., Vance, J. M., Ito, A., & Yao, T.-P. (2003). The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress. Cell. https://doi.org/10.1016/s0092-8674(03)00939-5
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