Assembly chaperone Nas6 selectively destabilizes 26S proteasomes with defective regulatory particle-core particle interfaces.

Warnock, Jennifer L; Jobin, Gabriel W; Kumar, Sandhya; Tomko, Robert J

Warnock, Jennifer L; Jobin, Gabriel W; Kumar, Sandhya; Tomko, Robert J.

Afiliación

Warnock JL; Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, Florida, USA.
Jobin GW; Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, Florida, USA.
Kumar S; Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, Florida, USA.
Tomko RJ; Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, Florida, USA. Electronic address: robert.tomko@med.fsu.edu.

J Biol Chem ; 299(2): 102894, 2023 02.

Article en En | MEDLINE | ID: mdl-36634850

Asunto(s)

Chaperonas Moleculares; Complejo de la Endopetidasa Proteasomal; Proteínas de Saccharomyces cerevisiae; ATPasas Asociadas con Actividades Celulares Diversas/metabolismo; Chaperonas Moleculares/metabolismo; Complejo de la Endopetidasa Proteasomal/metabolismo; Saccharomyces cerevisiae/metabolismo; Proteínas de Saccharomyces cerevisiae/metabolismo

Palabras clave

26S proteasome; assembly; chaperone; macromolecular complex; proteolysis; quality control; ubiquitin

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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Chaperonas Moleculares / Proteínas de Saccharomyces cerevisiae / Complejo de la Endopetidasa Proteasomal Idioma: En Revista: J Biol Chem Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos

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