The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity
Open accessAbstract
Huntington's disease is caused by an expanded polyglutamine tract in huntingtin protein, leading to accumulation of huntingtin in the nuclei of striatal neurons. The 18 amino-acid amino-terminus of huntingtin is an amphipathic alpha helical membrane-binding domain that can reversibly target to vesicles and the endoplasmic reticulum (ER). The association of huntingtin to the ER is affected by ER stress. A single point mutation in huntingtin 1-18 predicted to disrupt this helical structure displayed striking phenotypes of complete inhibition of polyglutamine-mediated aggregation, increased huntingtin nuclear accumulation and greatly increased mutant huntingtin toxicity in a striatal-derived mouse cell line. Huntingtin vesicular interaction mediated by 1-18 is specific to late endosomes and autophagic vesicles. We propose that huntingtin has a normal biological function as an ER-associated protein that can translocate to the nucleus and back out in response to ER stress or other events. The increased nuclear entry of mutant huntingtin due to loss of ER-targeting results in increased toxicity.
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Cites
Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979
Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes
Zuccato, C., Tartari, M., Crotti, A., Goffredo, D., Valenza, M., Conti, L., Cataudella, T., Leavitt, B. R., Hayden, M. R., Timmusk, T., et al. (2003) · Nature Genetics · doi:10.1038/ng1219 · Cited by 979
Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
DiFiglia, M., Sapp, E., Chase, K., Schwarz, C., Meloni, A., Young, C., Martin, E., Vonsattel, J.-P., Carraway, R., Reeves, S. A., et al. (1995) · Neuron · doi:10.1016/0896-6273(95)90346-1 · Cited by 749 · cited 1×
“This localization appeared similar to what has been reported for huntingtin by immunofluorescence in STHdh cells (19,22) and human neurons (13).”
ResultComparative Genomics, Evolution and Origins of the Nuclear Envelope and Nuclear Pore Complex
Mans, B., Anantharaman, V., Aravind, L., & Koonin, E. V. (2004) · Cell Cycle · doi:10.4161/cc.3.12.1316 · Cited by 304
Detection of Autophagy in Tissue by Standard Immunohistochemistry: Possibilities and Limitations
Martinet, W., Meyer, G. R. Y. D., Andries, L., Herman, A. G., & Kockx, M. M. (2006) · Autophagy · doi:10.4161/auto.2217 · Cited by 61
Cited by
Doherty, G. J., & McMahon, H. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081307.110540 · Cited by 3,075
Bates, G. P., Dorsey, R., Gusella, J. F., Hayden, M. R., Kay, C., Leavitt, B. R., Nance, M., Ross, C. A., Scahill, R. I., Wetzel, R., et al. (2015) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2015.5 · Cited by 1,641
Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease
Martinez-Vicente, M., Talloczy, Z., Wong, E., Tang, G., Koga, H., Kaushik, S., de Vries, R., Arias, E., Harris, S., Sulzer, D., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2528 · Cited by 885
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
Repeat expansion disease: progress and puzzles in disease pathogenesis
La Spada, A. R., & Taylor, J. P. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2748 · Cited by 488
Self-citation
Metadata
- Authors
- Atwal, R. S., Xia, J., Pinchev, D., Taylor, J., Epand, R. M., & Truant, R.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-08-08
- Volume
- 16
- Issue
- 21
- Pages
- 2600-2615
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2125054419
- Cited by
- 387
- References
- 5
- FWCI
- 6.77
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Atwal, R. S., Xia, J., Pinchev, D., Taylor, J., Epand, R. M., & Truant, R. (2007). Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Human Molecular Genetics. https://doi.org/10.1093/hmg/ddm217
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
