PMID- 28237106 OWN - NLM STAT- MEDLINE DCOM- 20170815 LR - 20180920 IS - 1557-7988 (Electronic) IS - 0076-6879 (Linking) VI - 588 DP - 2017 TI - Methods to Study Chaperone-Mediated Autophagy. PG - 283-305 LID - S0076-6879(16)30372-X [pii] LID - 10.1016/bs.mie.2016.10.009 [doi] AB - Chaperone-mediated autophagy (CMA), a selective form of degradation of cytosolic proteins in lysosomes, contributes to maintenance of proteostasis and to the cellular adaptation to stress. CMA substrates are selectively recognized and delivered by a cytosolic chaperone to the lysosomal surface, where, upon unfolding, they are internalized through a membrane translocation complex. Defective or dysfunctional CMA has been associated with human pathologies such as neurodegeneration, cancer, immunodeficiency, or diabetes, increasing the overall interest in methods to monitor this selective autophagic pathway. In this chapter, we review the different experimental approaches used to evaluate CMA activity in different organs from animals or in cell cultures in vitro. CI - (c) 2017 Elsevier Inc. All rights reserved. FAU - Arias, E AU - Arias E AD - Institute for Aging Studies, Albert Einstein College of Medicine, Bronx, NY, United States. Electronic address: esperanza.arias-perez@einstein.yu.edu. LA - eng GR - P30 AG038072/AG/NIA NIH HHS/United States PT - Journal Article PT - Research Support, N.I.H., Extramural PT - Research Support, Non-U.S. Gov't PT - Review DEP - 20161118 PL - United States TA - Methods Enzymol JT - Methods in enzymology JID - 0212271 RN - 0 (Molecular Chaperones) SB - IM MH - Animals MH - *Autophagy MH - Biochemistry/methods MH - Humans MH - Lysosomes/*metabolism MH - Molecular Chaperones/*metabolism MH - Proteolysis OTO - NOTNLM OT - Autophagy OT - Chemical modulators OT - Fluorescent reporters OT - Lysosomes OT - Organelle isolation EDAT- 2017/02/27 06:00 MHDA- 2017/08/16 06:00 CRDT- 2017/02/27 06:00 PHST- 2017/02/27 06:00 [entrez] PHST- 2017/02/27 06:00 [pubmed] PHST- 2017/08/16 06:00 [medline] AID - S0076-6879(16)30372-X [pii] AID - 10.1016/bs.mie.2016.10.009 [doi] PST - ppublish SO - Methods Enzymol. 2017;588:283-305. doi: 10.1016/bs.mie.2016.10.009. Epub 2016 Nov 18.