Hugging tight in Huntington's

Mitochondrial fission-fusion and trafficking are altered in the fatal neurodegenerative disorder Huntington's disease. Huntingtin is now shown to function directly in these processes by binding the mitochondrial fission factor dynamin-related protein-1 (DRP1). Mutant huntingtin binds more tight...

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Veröffentlicht in:	Nature medicine 2011-03, Vol.17 (3), p.245-246
Hauptverfasser:	Johri, Ashu, Chaturvedi, Rajnish K, Beal, M Flint
Format:	Artikel
Sprache:	eng
Schlagworte:	631/378/1689/1558 692/420 Binding sites Biomedical and Life Sciences Biomedicine Cancer Research Care and treatment GTP Phosphohydrolases - metabolism Humans Huntingtin Protein Huntington Disease - genetics Huntington Disease - metabolism Huntington Disease - physiopathology Huntington's chorea Huntingtons disease Infectious Diseases Metabolic Diseases Microtubule-Associated Proteins - metabolism Mitochondria Mitochondrial Proteins - metabolism Molecular Medicine Mutation Nerve Tissue Proteins - metabolism Nerve Tissue Proteins - physiology Neurosciences news-and-views Nuclear Proteins - metabolism Nuclear Proteins - physiology Physiological aspects Protein Binding Proteins
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Beschreibung
Zusammenfassung:	Mitochondrial fission-fusion and trafficking are altered in the fatal neurodegenerative disorder Huntington's disease. Huntingtin is now shown to function directly in these processes by binding the mitochondrial fission factor dynamin-related protein-1 (DRP1). Mutant huntingtin binds more tightly to DRP1, leading to increased mitochondrial fission and neuronal death, highlighting DRP1 as a potential therapeutic target in Huntington's disease ( pages 377–382 ).
ISSN:	1078-8956 1546-170X
DOI:	10.1038/nm0311-245