PMID- 20643207
OWN - NLM
STAT- MEDLINE
DCOM- 20120409
LR  - 20240511
IS  - 1095-953X (Electronic)
IS  - 0969-9961 (Print)
IS  - 0969-9961 (Linking)
VI  - 43
IP  - 1
DP  - 2011 Jul
TI  - Chaperone-mediated autophagy dysfunction in the pathogenesis of 
      neurodegeneration.
PG  - 29-37
LID - 10.1016/j.nbd.2010.07.006 [doi]
AB  - Chaperone-mediated autophagy (CMA) contributes to selective degradation of 
      individual soluble proteins in lysosomes. Unique to this type of autophagy is the 
      fact that proteins reach the lysosomal lumen for degradation by directly crossing 
      the lysosomal membrane, in contrast with the vesicle-mediated delivery 
      characteristic of the other types of autophagy. These two 
      characteristics--selective targeting and direct translocation of 
      substrates--determine the contribution of CMA to different physiological 
      functions and the type of pathological conditions associated with CMA 
      dysfunction. In this review, we briefly revise recent findings on the molecular 
      mechanisms behind CMA function, and describe the physiological relevance of the 
      selective lysosomal degradation through this pathway. We also comment on the 
      cellular consequences of CMA malfunction and on the connections already 
      established between CMA dysfunction and different human disorders, with special 
      emphasis on neurodegenerative diseases. This article is part of a Special Issue 
      entitled "Autophagy and protein degradation in neurological diseases."
CI  - Copyright (c) 2010 Elsevier Inc. All rights reserved.
FAU - Koga, Hiroshi
AU  - Koga H
AD  - Department of Developmental and Molecular Biology, Institute for Aging Research, 
      Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY, USA. 
      ana-maria.cuervo@einstein.yu.edu
FAU - Cuervo, Ana Maria
AU  - Cuervo AM
LA  - eng
GR  - P50 NS038370/NS/NINDS NIH HHS/United States
GR  - NS038370/NS/NINDS NIH HHS/United States
GR  - P01 DK041918/DK/NIDDK NIH HHS/United States
GR  - AG031782/AG/NIA NIH HHS/United States
GR  - R37 AG021904/AG/NIA NIH HHS/United States
GR  - P01 AG031782-01A18475/AG/NIA NIH HHS/United States
GR  - R01 AG021904-09/AG/NIA NIH HHS/United States
GR  - R01 AG021904/AG/NIA NIH HHS/United States
GR  - DK041918/DK/NIDDK NIH HHS/United States
GR  - P01 AG031782/AG/NIA NIH HHS/United States
GR  - AG021904/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 - 20100717
PL  - United States
TA  - Neurobiol Dis
JT  - Neurobiology of disease
JID - 9500169
RN  - 0 (Molecular Chaperones)
SB  - IM
MH  - Autophagy/*physiology
MH  - Humans
MH  - Molecular Chaperones/*physiology
MH  - Nerve Degeneration/*etiology/*metabolism/pathology
MH  - Neurodegenerative Diseases/*etiology/*metabolism/pathology
PMC - PMC2998583
MID - NIHMS224242
EDAT- 2010/07/21 06:00
MHDA- 2012/04/10 06:00
PMCR- 2012/07/01
CRDT- 2010/07/21 06:00
PHST- 2010/06/09 00:00 [received]
PHST- 2010/07/02 00:00 [revised]
PHST- 2010/07/09 00:00 [accepted]
PHST- 2010/07/21 06:00 [entrez]
PHST- 2010/07/21 06:00 [pubmed]
PHST- 2012/04/10 06:00 [medline]
PHST- 2012/07/01 00:00 [pmc-release]
AID - S0969-9961(10)00230-5 [pii]
AID - 10.1016/j.nbd.2010.07.006 [doi]
PST - ppublish
SO  - Neurobiol Dis. 2011 Jul;43(1):29-37. doi: 10.1016/j.nbd.2010.07.006. Epub 2010 
      Jul 17.