Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.
FEBS Lett
; 588(1): 151-9, 2014 Jan 03.
Article
en En
| MEDLINE
| ID: mdl-24291262
ABSTRACT
Neurodegenerative disorders such as Huntington's disease are hallmarked by neuronal intracellular inclusion body formation. Whether proteasomes are irreversibly recruited into inclusion bodies in these protein misfolding disorders is a controversial subject. In addition, it has been proposed that the proteasomes may become clogged by the aggregated protein fragments, leading to impairment of the ubiquitin-proteasome system. Here, we show by fluorescence pulse-chase experiments in living cells that proteasomes are dynamically and reversibly recruited into inclusion bodies. As these recruited proteasomes remain catalytically active and accessible to substrates, our results challenge the concept of proteasome sequestration and impairment in Huntington's disease, and support the reported absence of proteasome impairment in mouse models of Huntington's disease.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Cuerpos de Inclusión
/
Enfermedad de Huntington
/
Complejo de la Endopetidasa Proteasomal
Límite:
Animals
/
Female
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Humans
/
Male
Idioma:
En
Revista:
FEBS Lett
Año:
2014
Tipo del documento:
Article
País de afiliación:
Países Bajos