Chaperones in autophagy

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Cells continuously turn over proteins through cycles of synthesis and degradation in order to maintain a functional proteome and to exert a tight control in the levels of regulatory proteins. Selective degradation of proteins was initially thought to be an exclusive function of the ubiquitin-proteasome system, however, over the years, the contribution of lysosomes to this selective degradation, through the process of autophagy, has become consolidated. In this context, molecular chaperones, classically associated with protein folding, unfolding and assembling have been revealed as important modulators of selectivity during the autophagic process. Here, we review this relatively new role of chaperones in mediating selective autophagy and comment on how alterations of this function can lead to human pathologies associated to proteotoxicity.

Original languageEnglish (US)
Pages (from-to)484-493
Number of pages10
JournalPharmacological Research
Volume66
Issue number6
DOIs
StatePublished - Dec 2012

Fingerprint

Autophagy
Protein Unfolding
Molecular Chaperones
Protein Folding
Proteasome Endopeptidase Complex
Proteome
Ubiquitin
Lysosomes
Proteolysis
Proteins
Pathology

Keywords

  • Aging
  • Chaperones
  • Lysosomes
  • Membrane proteins
  • Protein degradation

ASJC Scopus subject areas

  • Pharmacology

Cite this

Chaperones in autophagy. / Kaushik, Susmita; Cuervo, Ana Maria.

In: Pharmacological Research, Vol. 66, No. 6, 12.2012, p. 484-493.

Research output: Contribution to journalArticle

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