title: Insights into the relationship between the proteasome and autophagy in human and yeast cells.
abstract: In eukaryotes, the ubiquitin-proteasome system (UPS) and autophagy are two major intracellular protein degradation pathways. Several lines of evidence support the emerging concept of a coordinated and complementary relationship between these two processes, and a particularly interesting finding is that the inhibition of the proteasome induces autophagy. Yet, there is limited knowledge of the regulation of the UPS by autophagy. In this study, we show that the disruption of ATG5 and ATG32 genes in yeast cells under both nutrient-deficient conditions as well as stress that causes mitochondrial dysfunction leads to an activation of proteasome. The same scenario occurs after pharmacological inhibition of basal autophagy in cultured human cells. Our findings underline the view that the two processes are interconnected and tend to compensate, to some extent, for each other's functions.
authors.affiliation: CNRS, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France; Université de Bordeaux, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France.
authors.forename: Axel
authors.initials: A
authors.lastname: Athané
authors.affiliation: CNRS, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France; Université de Bordeaux, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France.
authors.forename: Anthony
authors.initials: A
authors.lastname: Buisson
authors.affiliation: CNRS, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France; Université de Bordeaux, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France.
authors.forename: Marion
authors.initials: M
authors.lastname: Challier
authors.affiliation: CNRS, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France; Université de Bordeaux, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France.
authors.forename: Florian
authors.initials: F
authors.lastname: Beaumatin
authors.affiliation: CNRS, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France; Université de Bordeaux, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France.
authors.forename: Stéphen
authors.initials: S
authors.lastname: Manon
authors.affiliation: Comenius University, Faculty of Natural Sciences, Department of Biochemistry, Mlynská dolina CH1 84215, Bratislava, Slovak Republic.
authors.forename: Ingrid
authors.initials: I
authors.lastname: Bhatia-Kiššová
authors.affiliation: CNRS, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France; Université de Bordeaux, IBGC, UMR5095, 1 rue Camille Saint-Saëns, F-33000 Bordeaux, France. Electronic address: n.camougrand@ibgc.cnrs.fr.
authors.forename: Nadine
authors.initials: N
authors.lastname: Camougrand
mesh_terms: D001343:Autophagy; D000071187:Autophagy-Related Protein 5; D000071183:Autophagy-Related Proteins; D015870:Gene Expression; D045325:HCT116 Cells; D006367:HeLa Cells; D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000502:physiology*; D018160:Receptors, Cytoplasmic and Nuclear / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism
chemical_list: C102268:ATG5 protein, S cerevisiae; C543183:Atg32 protein, S cerevisiae; D000071187:Autophagy-Related Protein 5; D000071183:Autophagy-Related Proteins; D018160:Receptors, Cytoplasmic and Nuclear; D029701:Saccharomyces cerevisiae Proteins; D044767:Ubiquitin-Protein Ligases; D046988:Proteasome Endopeptidase Complex
keywords: Autophagy; Human cell lines; Mitophagy; Proteasome; Yeast