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Cell Res. 2014 Jan;24(1):92-104. doi: 10.1038/cr.2013.153. Epub 2013 Nov 26.

Chaperone-mediated autophagy: roles in disease and aging.

Author information

1
Department of Developmental and Molecular Biology, Institute for Aging Studies, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Chanin Building 504, Bronx, NY 10461, USA.
2
School of Biological Sciences, Nanyang Technological University, SBS-03n-05, 60 Nanyang Drive, Singapore 637551, Singapore.

Abstract

This review focuses on chaperone-mediated autophagy (CMA), one of the proteolytic systems that contributes to degradation of intracellular proteins in lysosomes. CMA substrate proteins are selectively targeted to lysosomes and translocated into the lysosomal lumen through the coordinated action of chaperones located at both sides of the membrane and a dedicated protein translocation complex. The selectivity of CMA permits timed degradation of specific proteins with regulatory purposes supporting a modulatory role for CMA in enzymatic metabolic processes and subsets of the cellular transcriptional program. In addition, CMA contributes to cellular quality control through the removal of damaged or malfunctioning proteins. Here, we describe recent advances in the understanding of the molecular dynamics, regulation and physiology of CMA, and discuss the evidence in support of the contribution of CMA dysfunction to severe human disorders such as neurodegeneration and cancer.

PMID:
24281265
PMCID:
PMC3879702
DOI:
10.1038/cr.2013.153
[Indexed for MEDLINE]
Free PMC Article

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