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

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dc.contributor.authorHormazábal, Juan
dc.contributor.authorSaavedra, Francisco
dc.contributor.authorEspinoza, Claudia
dc.contributor.authorMartínez, Nicolás
dc.contributor.authorCruces, Tatiana
dc.contributor.authorIván, Alfaro
dc.contributor.authorLoyola, Alejandra
dc.date.accessioned2022-03-08T21:06:53Z
dc.date.available2022-03-08T21:06:53Z
dc.date.issued2022
dc.description.abstractAlthough 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.es
dc.description.versionVersión publicadaes
dc.identifier.citationHormazabal J, Saavedra F, Espinoza-Arratia C, Martinez NW, Cruces T, Alfaro IE, Loyola A. Chaperone mediated autophagy contributes to the newly synthesized histones H3 and H4 quality control. Nucleic Acids Res. 2022 Feb 28;50(4):1875-1887. doi:0.1093/nar/gkab1296es
dc.identifier.urihttps://doi.org/10.1093/nar/gkab1296es
dc.identifier.urihttp://hdl.handle.net/11447/5681
dc.language.isoenes
dc.subjectHistones / metabolismes
dc.subjectHistone Acetyltransferaseses
dc.subjectChickens / metabolismes
dc.subjectNucleic acidses
dc.subjectsynthesized histoneses
dc.titleChaperone mediated autophagy contributes to the newly synthesized histones H3 and H4 quality controles
dc.typeArticlees
dcterms.sourceNucleic Acids Researches

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