Chaperone mediated autophagy contributes to the newly synthesized histones H3 and H4 quality control

Juan Hormazabal, Francisco Saavedra, Claudia Espinoza-Arratia, Nicolas W. Martinez, Tatiana Cruces, Iván E. Alfaro*, Alejandra Loyola*

*Autor correspondiente de este trabajo

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

11 Citas (Scopus)

Resumen

Although there are several pathways to ensure that proteins are folded properly in the cell, little is known about the molecular mechanisms regulating histone folding and proteostasis. In this work, we identified that chaperone-mediated autophagy (CMA) is the main pathway involved in the degradation of newly synthesized histones H3 and H4. This degradation is finely regulated by the interplay between HSC70 and tNASP, two histone interacting proteins. tNASP stabilizes histone H3 levels by blocking the direct transport of histone H3 into lysosomes. We further demonstrate that CMA degrades unfolded histone H3. Thus, we reveal that CMA is the main degradation pathway involved in the quality control of histone biogenesis, evidencing an additional mechanism in the intricate network of histone cellular proteostasis.

Idioma originalInglés
Páginas (desde-hasta)1875-1887
Número de páginas13
PublicaciónNucleic Acids Research
Volumen50
N.º4
DOI
EstadoPublicada - 2022

Nota bibliográfica

Publisher Copyright:
© 2022 The Author(s). Published by Oxford University Press on behalf of Nucleic Acids Research.

Áreas temáticas de ASJC Scopus

  • Genética

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