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The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction

Opened Access The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction

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Autor: Sot, Begoña
Rubio Muñoz, Alejandra
Leal Quintero, Ahundrey
Martínez Sabando, Javier
Marcilla, Miguel
Roodveldt, Cintia
Valpuesta, José M.
Fecha: 2017
Publicado en: Scientific Reports, 7, 40859-.
Tipo de documento: Artículo
Resumen: The eukaryotic chaperonin CCT (chaperonin containing TCP-1) uses cavities built into its double-ring structure to encapsulate and to assist folding of a large subset of proteins. CCT can inhibit amyloid fibre assembly and toxicity of the polyQ extended mutant of huntingtin, the protein responsible for Huntington's disease. This raises the possibility that CCT modulates other amyloidopathies, a still-unaddressed question. We show here that CCT inhibits amyloid fibre assembly of α-synuclein A53T, one of the mutants responsible for Parkinson's disease. We evaluated fibrillation blockade in α-synuclein A53T deletion mutants and CCT interactions of full-length A53T in distinct oligomeric states to define an inhibition mechanism specific for α-synuclein. CCT interferes with fibre assembly by interaction of its CCT and CCT 3 subunits with the A53T central hydrophobic region (NAC). This interaction is specific to NAC conformation, as it is produced once soluble α-synuclein A53T oligomers form...
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Cita: Sot, B., Rubio Muñoz, A., Leal Quintero, A., Martínez Sabando, J., Marcilla, M., Roodveldt, C. y Valpuesta, J.M. (2017). The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction. Scientific Reports, 7, 40859-.
Tamaño: 1.526Mb
Formato: PDF

URI: http://hdl.handle.net/11441/64293

DOI: 10.1038/srep40859

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