The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Huntingtin Is Present in the Nucleus, Interacts with the Transcriptional Corepressor C-terminal Binding Protein, and Represses Transcription
Open accessAbstract
Huntingtin is a protein of unknown function that contains a polyglutamine tract, which is expanded in patients with Huntington's disease (HD). We investigated the localization and a potential function for huntingtin in the nucleus. In human fibroblasts from normal and HD patients, huntingtin localized diffusely in the nucleus and in subnuclear compartments identified as speckles, promyelocytic leukemia protein bodies, and nucleoli. Huntingtin-positive nuclear bodies redistributed after treatment with sodium butyrate. By Western blot, purified nuclei had low levels of full-length huntingtin compared with the cytoplasm but contained high levels of N- and C-terminal huntingtin fragments, which tightly bound the nuclear matrix. Full-length huntingtin co-immunoprecipitated with the transcriptional corepressor C-terminal binding protein, and polyglutamine expansion in huntingtin reduced this interaction. Full-length wild-type and mutant huntingtin repressed transcription when targeted to DNA. Truncated N-terminal mutant huntingtin repressed transcription, whereas the corresponding wild-type fragment did not repress transcription. We speculate that wild-type huntingtin may function in the nucleus in the assembly of nuclear matrix-bound protein complexes involved with transcriptional repression and RNA processing. Proteolysis of mutant huntingtin may alter nuclear functions by disrupting protein complexes and inappropriately repressing transcription in HD.
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Cites
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Self-citationHuntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
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Cited by
Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
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Molecular Mechanisms and Potential Therapeutical Targets in Huntington's Disease
Zuccato, C., Valenza, M., & Cattaneo, E. (2010) · Physiological Reviews · doi:10.1152/physrev.00041.2009 · Cited by 848
Sp1 and TAFII130 Transcriptional Activity Disrupted in Early Huntington's Disease
Dunah, A. W., Jeong, H., Griffin, A., Kim, Y.-M., Standaert, D. G., Hersch, S. M., Mouradian, M. M., Young, A. B., Tanese, N., & Krainc, D. (2002) · Science · doi:10.1126/science.1072613 · Cited by 708
Self-citationNormal huntingtin function: an alternative approach to Huntington's disease
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Huntingtin–protein interactions and the pathogenesis of Huntington's disease
Li, S.-H., & Li, X.-J. (2004) · Trends in Genetics · doi:10.1016/j.tig.2004.01.008 · Cited by 548
Metadata
- Authors
- Kegel, K. B., Meloni, A. R., Yi, Y., Kim, Y. J., Doyle, E., Cuiffo, B. G., Sapp, E., Wang, Y., Qin, Z.-H., Chen, J. D., Nevins, J. R., Aronin, N., & DiFiglia, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-03
- Volume
- 277
- Issue
- 9
- Pages
- 7466-7476
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2132082381
- Cited by
- 287
- References
- 53
- FWCI
- 7.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kegel, K. B., Meloni, A. R., Yi, Y., Kim, Y. J., Doyle, E., Cuiffo, B. G., Sapp, E., Wang, Y., Qin, Z.-H., Chen, J. D., Nevins, J. R., Aronin, N., & DiFiglia, M. (2002). Huntingtin Is Present in the Nucleus, Interacts with the Transcriptional Corepressor C-terminal Binding Protein, and Represses Transcription. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m103946200
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