PMID- 16585521
OWN - NLM
STAT- MEDLINE
DCOM- 20060609
LR  - 20231213
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 103
IP  - 15
DP  - 2006 Apr 11
TI  - Consequences of the selective blockage of chaperone-mediated autophagy.
PG  - 5805-10
AB  - Chaperone-mediated autophagy (CMA) is a selective pathway for the degradation of 
      cytosolic proteins in lysosomes. CMA declines with age because of a decrease in 
      the levels of lysosome-associated membrane protein (LAMP) type 2A, a lysosomal 
      receptor for this pathway. We have selectively blocked the expression of LAMP-2A 
      in mouse fibroblasts in culture and analyzed the cellular consequences of reduced 
      CMA activity. CMA-defective cells maintain normal rates of long-lived protein 
      degradation by up-regulating macroautophagy, the major form of autophagy. 
      Constitutive up-regulation of macroautophagy is unable, however, to compensate 
      for all CMA functions. Thus, CMA-defective cells are more sensitive to stressors, 
      suggesting that, although protein turnover is maintained, the selectivity of CMA 
      is necessary as part of the cellular response to stress. Our results also denote 
      the existence of cross-talk among different forms of autophagy.
FAU - Massey, Ashish C
AU  - Massey AC
AD  - Department of Anatomy and Structural Biology, Marion Bessin Liver Research 
      Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Ullmann 
      Building, Room 611, Bronx, NY 10461, USA.
FAU - Kaushik, Susmita
AU  - Kaushik S
FAU - Sovak, Guy
AU  - Sovak G
FAU - Kiffin, Roberta
AU  - Kiffin R
FAU - Cuervo, Ana Maria
AU  - Cuervo AM
LA  - eng
GR  - R01 AG021904/AG/NIA NIH HHS/United States
GR  - T32 AG023475/AG/NIA NIH HHS/United States
GR  - R37 AG021904/AG/NIA NIH HHS/United States
GR  - T32AG023475/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
DEP - 20060403
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Lysosomal Membrane Proteins)
RN  - EC 3.6.1.- (Chaperonins)
SB  - IM
MH  - 3T3 Cells
MH  - Animals
MH  - Autophagy
MH  - Cells, Cultured
MH  - Chaperonins/antagonists & inhibitors/*physiology
MH  - Fibroblasts/cytology/physiology
MH  - Kinetics
MH  - Lysosomal Membrane Proteins/physiology
MH  - Lysosomes/*physiology/ultrastructure
MH  - Mice
MH  - RNA Interference
PMC - PMC1458654
COIS- Conflict of interest statement: No conflicts declared.
EDAT- 2006/04/06 09:00
MHDA- 2006/06/10 09:00
PMCR- 2006/10/11
CRDT- 2006/04/06 09:00
PHST- 2006/04/06 09:00 [pubmed]
PHST- 2006/06/10 09:00 [medline]
PHST- 2006/04/06 09:00 [entrez]
PHST- 2006/10/11 00:00 [pmc-release]
AID - 0507436103 [pii]
AID - 1805 [pii]
AID - 10.1073/pnas.0507436103 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2006 Apr 11;103(15):5805-10. doi: 
      10.1073/pnas.0507436103. Epub 2006 Apr 3.