Chaperone-mediated autophagy : roles in disease and aging
Cuervo, Ana Maria
Date of Issue2014
School of Biological Sciences
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 in both sides of the membrane and a dedicate 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 evidences in support of the contribution of CMA dysfunction to severe human disorders such as neurodegeneration and cancer.
DRNTU::Science::Biological sciences::Molecular biology
© 2014 The Authors. This is the author created version of a work that has been peer reviewed and accepted for publication in Cell Research, published by Nature Publishing Group on behalf of The Authors. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [Article DOI: http://dx.doi.org/10.1038/cr.2013.153].