Chaperone-mediated autophagy

Eloy Bejarano-Fernandez, Ana Maria Cuervo

Research output: Contribution to journalReview articlepeer-review

115 Scopus citations


Continuous renewal of intracellular components is required to preserve cellular functionality. In fact, failure to timely turnover proteins and organelles leads often to cell death and disease. Different pathways contribute to the degradation of intracellular components in lysosomes or autophagy. In this review, we focus on chaperone-mediated autophagy (CMA), a selective form of autophagy that modulates the turnover of a specific pool of soluble cytosolic proteins. Selectivity in CMA is conferred by the presence of a targeting motif in the cytosolic substrates that, upon recognition by a cytosolic chaperone, determines delivery to the lysosomal surface. Substrate proteins undergo unfolding and translocation across the lysosomal membrane before reaching the lumen, where they are rapidly degraded. Better molecular characterization of the different components of this pathway in recent years, along with the development of transgenic models with modified CMA activity and the identification of CMA dysfunction in different severe human pathologies and in aging, are all behind the recent regained interest in this catabolic pathway.

Original languageEnglish (US)
Pages (from-to)29-39
Number of pages11
JournalProceedings of the American Thoracic Society
Issue number1
StatePublished - Feb 15 2010


  • Aging
  • Lysosomes
  • Membrane proteins
  • Proteases
  • Protein translocation

ASJC Scopus subject areas

  • Pulmonary and Respiratory Medicine


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