Regular ArticlePolyglutamine Repeat Length-Dependent Proteolysis of Huntingtin
References (43)
Transcriptional dysregulation in Huntington's disease
Trends Neurosci.
(2000)- et al.
Huntingtin: A single bait hooks many species
Curr. Opin. Neurobiol.
(1998) - et al.
Huntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domain
J. Biol. Chem.
(2000) - et al.
Huntington's disease: Translating a CAG repeat into a pathogenic mechanism
Curr. Opin. Neurobiol.
(1996) - et al.
Nuclear targeting of mutant huntingtin increases toxicity
Mol. Cell. Neurosci.
(1999) - et al.
Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
Cell
(1998) Nuclear inclusions in glutamine repeat disorders: Are they pernicious, coincidental, or beneficial?
Cell
(1998)- et al.
Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
J. Biol. Chem.
(1998) - et al.
Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells
J. Biol. Chem.
(2000) - et al.
The nuclear pore complex: Mediator of translocation between nucleus and cytoplasm
J. Cell. Sci.
(2000)
The likelihood of being affected with Huntington disease by a particular age, for a specific CAG size
Am. J. Hum. Genet.
Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture
Hum. Mol. Genet.
Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
Nature Genet.
Trinucleotide repeats: Mechanisms and pathophysiology
Annu. Rev. Genomics Hum. Genet.
Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
Science
Relationship between trinucleotide repeats and neuropathological changes in Huntington's disease
Ann. Neurol.
Nucleocytoplasmic transport
Science
Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract
Nature Genet.
Huntington's disease
Cold Spring Harbor Symp. Quant. Biol.
In vitro evidence for both the nucleus and cytoplasm as subcellular sites of pathogenesis in Huntington's disease
Hum. Mol. Genet.
HIP1, a human homologue of S-cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain
Nature Genet.
Cited by (39)
Minimotifs dysfunction is pervasive in neurodegenerative disorders
2018, Alzheimer's and Dementia: Translational Research and Clinical InterventionsCitation Excerpt :These fragments are present in the amyloid fibrils of patients with Familial British dementia [169–171]. Several proteases cleave HTT at minimotifs producing peptide aggregation and neurotoxic peptides [172–176]. Minimotifs are important in protein trafficking to and from organelles and are relevant to several NDs [1,177,178].
A large scale huntingtin protein interaction network implicates RHO GTPase signaling pathways in huntington disease
2014, Journal of Biological ChemistryAssessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides
2011, Biophysical ChemistryCitation Excerpt :Expanded polyglutamine tracts have all the hallmarks of being intrinsically disordered regions [4–9] although this does not translate into their classification as canonical random coils [10]. Polyglutamine regions destabilize their host protein thereby increasing its susceptibility to proteolysis [11–21]. Products of proteolysis are rich in unprocessed polyglutamine regions [22,23], which are prone to aggregation [6,24–30] as well as recruitment and sequestration [6,31,32] of polyglutamine-rich regions from other proteins, specifically transcription factors [33–46].
Cysteine proteases bleomycin hydrolase and cathepsin Z mediate N-terminal proteolysis and toxicity of mutant huntingtin
2011, Journal of Biological ChemistryMolecular biology of Huntington's disease
2011, Handbook of Clinical NeurologyProteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in huntington disease
2010, Journal of Biological Chemistry
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These authors contributed equally to this effort.