The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases
Open accessAbstract
Huntington's disease (HD) is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) tract in the huntingtin (htt) protein. Mutant htt toxicity is exposed after htt cleavage by caspases and other proteases release NH2-terminal fragments containing the polyQ expansion. Here, we show htt interacts and colocalizes with cdk5 in cellular membrane fractions. Cdk5 phosphorylates htt at Ser434, and this phosphorylation reduces caspase-mediated htt cleavage at residue 513. Reduced mutant htt cleavage resulting from cdk5 phosphorylation attenuated aggregate formation and toxicity in cells expressing the NH2-terminal 588 amino acids (htt588) of mutant htt. Cdk5 activity is reduced in the brains of HD transgenic mice compared with controls. This result can be accounted for by the polyQ-expanded htt fragments reducing the interaction between cdk5 and its activator p35. These data predict that the ability of cdk5 phosphorylation to protect against htt cleavage, aggregation, and toxicity is compromised in cells expressing toxic fragments of htt.
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Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347
Self-citationHuntingtin 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 2×
“…O G Y © The Rockefeller University Press $8.00 The Journal of Cell Biology, Vol. 169, No. 4, May 23, 2005 647–656 http://www.jcb.org/cgi/doi/10.1083/jcb.200412071 JCB: ARTICLE JCB 647 Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: implications for mutant huntingtin toxicity”
BackgroundInfluential
Cited by
The roles of intracellular protein-degradation pathways in neurodegeneration
Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625
Self-citationMolecular 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
Rapamycin alleviates toxicity of different aggregate-prone proteins
Berger, Z., Ravikumar, B., Menzies, F. M., Oroz, L. G., Underwood, B. R., Pangalos, M. N., Schmitt, I., Wullner, U., Evert, B. O., O'Kane, C. J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi458 · Cited by 657
Self-citationNormal huntingtin function: an alternative approach to Huntington's disease
Cattaneo, E., Zuccato, C., & Tartari, M. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1806 · Cited by 657
Huntington’s Disease: Mechanisms of Pathogenesis and Therapeutic Strategies
Jimenez-Sanchez, M., Licitra, F., Underwood, B. R., & Rubinsztein, D. C. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024240 · Cited by 507
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Metadata
- Authors
- Luo, S., Vacher, C., Davies, J. E., & Rubinsztein, D. C.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2005-05-23
- Volume
- 169
- Issue
- 4
- Pages
- 647-656
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2141928432
- Cited by
- 195
- References
- 2
- FWCI
- 4.64
- Type
- journal article
- Language
- en
- Open access
- green
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- Luo, S., Vacher, C., Davies, J. E., & Rubinsztein, D. C. (2005). Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200412071
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