The ribosome-bound quality control complex: from aberrant peptide clearance to proteostasis maintenance

Autor: Quentin Defenouillère, Micheline Fromont-Racine
Přispěvatelé: Génétique des Interactions macromoléculaires, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), This work was supported by ANR-14-CE-10-0014-01 from the Agence Nationale de la Recherche, the Institut Pasteur, and the Centre National de la Recherche Scientifique. Q.D. was supported by a postdoctoral fellowship from the Fondation pour la Recherche Médicale (SPF20150934065)., ANR-14-CE10-0014,CLEANMD,Mécanismes moléculaires et impact de la voie de dégradation des ARNm nonsense (NMD) sur le transcriptome eucaryote.(2014), Génétique des Interactions macromoléculaires / Genetics of Macromolecular Interactions, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2017
Předmět:
0301 basic medicine
Proteasome Endopeptidase Complex
Saccharomyces cerevisiae Proteins
Translational quality control
Protein subunit
[SDV]Life Sciences [q-bio]
Ubiquitin-Protein Ligases
MESH: Proteolysis
Saccharomyces cerevisiae
Protein degradation
Biology
Proteomics
Ribosome
03 medical and health sciences
Aggregation
Protein Aggregates
RQC complex
MESH: Saccharomyces cerevisiae Proteins
Genetics
Animals
Humans
MESH: Animals
MESH: Humans
MESH: Proteasome Endopeptidase Complex
Ubiquitination
General Medicine
Ribosome Subunits
Large
Eukaryotic
MESH: Ubiquitin-Protein Ligases
MESH: Saccharomyces cerevisiae
Cell biology
MESH: Protein Aggregates
Cytosol
030104 developmental biology
Proteostasis
Proteasome
Biochemistry
MESH: Ribosome Subunits
Large
Eukaryotic
MESH: Protein Biosynthesis
Protein Biosynthesis
Proteolysis
MESH: Ubiquitination
MESH: Proteostasis
MESH: Molecular Chaperones
Molecular Chaperones
Zdroj: Current Genetics
Current Genetics, Springer Verlag, 2017, 63 (6), pp.997-1005. ⟨10.1007/s00294-017-0708-5⟩
Current Genetics, 2017, 63 (6), pp.997-1005. ⟨10.1007/s00294-017-0708-5⟩
ISSN: 1432-0983
0172-8083
DOI: 10.1007/s00294-017-0708-5⟩
Popis: International audience; Proteostasis in eukaryotes is maintained by compartment-specific quality control pathways, which enable the refolding or the degradation of defective polypeptides to prevent the toxicity that may arise from their aggregation. Among these processes, translational protein quality control is performed by the Ribosome-bound Quality Control complex (RQC), which recognizes nascent peptides translated from aberrant mRNAs, polyubiquitylates these aberrant peptides, extracts them from the stalled 60S subunit and finally escorts them to the proteasome for degradation. In this review, we focus on the mechanism of action of the RQC complex from stalled 60S binding to aberrant peptide delivery to the proteasome and describe the cellular consequences of a deficiency in the RQC pathway, such as aberrant protein aggregation. In addition, this review covers the recent discoveries concerning the role of cytosolic chaperones, as well as Tom1, to prevent the accumulation of aberrant protein aggregates in case of a deficiency in the RQC pathway.
Databáze: OpenAIRE
Externí odkaz: