PMID- 20797626
OWN - NLM
STAT- MEDLINE
DCOM- 20100920
LR  - 20230815
IS  - 1097-4164 (Electronic)
IS  - 1097-2765 (Print)
IS  - 1097-2765 (Linking)
VI  - 39
IP  - 4
DP  - 2010 Aug 27
TI  - Identification of regulators of chaperone-mediated autophagy.
PG  - 535-47
LID - 10.1016/j.molcel.2010.08.004 [doi]
AB  - Chaperone-mediated autophagy (CMA) is a selective mechanism for the degradation 
      of cytosolic proteins in lysosomes that contributes to cellular quality control 
      and becomes an additional source of amino acids when nutrients are scarce. A 
      chaperone complex delivers CMA substrates to a receptor protein at the lysosomal 
      membrane that assembles into multimeric translocation complexes. However, the 
      mechanisms regulating this process remain, for the most part, unknown. In this 
      work, we have identified two regulatory proteins, GFAP and EF1alpha, that mediate 
      a previously unknown inhibitory effect of GTP on CMA. GFAP stabilizes the 
      multimeric translocation complex against chaperone-mediated disassembly, whereas 
      GTP-mediated release of EF1alpha from the lysosomal membrane promotes 
      self-association of GFAP, disassembly of the CMA translocation complex, and the 
      consequent decrease in CMA. The dynamic interactions of these two proteins at the 
      lysosomal membrane unveil now a role for GTP as a negative regulator of CMA.
CI  - Copyright (c) 2010 Elsevier Inc. All rights reserved.
FAU - Bandyopadhyay, Urmi
AU  - Bandyopadhyay U
AD  - Department of Development and Molecular Biology, Institute for Aging Studies, 
      Albert Einstein College of Medicine, Bronx, NY 10461, USA.
FAU - Sridhar, Sunandini
AU  - Sridhar S
FAU - Kaushik, Susmita
AU  - Kaushik S
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  - R37 AG021904/AG/NIA NIH HHS/United States
GR  - R01 AG021904-09/AG/NIA NIH HHS/United States
GR  - P01 AG031782-03/AG/NIA NIH HHS/United States
GR  - TG32AG023475/AG/NIA NIH HHS/United States
GR  - T32 AG023475/AG/NIA NIH HHS/United States
GR  - AG031782/AG/NIA NIH HHS/United States
GR  - F31 AG034040/AG/NIA 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
PL  - United States
TA  - Mol Cell
JT  - Molecular cell
JID - 9802571
RN  - 0 (Glial Fibrillary Acidic Protein)
RN  - 0 (Lysosomal-Associated Membrane Protein 2)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptide Elongation Factor 1)
RN  - 0 (glial fibrillary astrocytic protein, mouse)
RN  - 86-01-1 (Guanosine Triphosphate)
SB  - IM
CIN - Mol Cell. 2010 Aug 27;39(4):485-6. PMID: 20797620
MH  - Animals
MH  - *Autophagy
MH  - Fibroblasts/*metabolism/pathology
MH  - Glial Fibrillary Acidic Protein
MH  - Guanosine Triphosphate/metabolism
MH  - Hepatocytes/*metabolism/pathology
MH  - Lysosomal-Associated Membrane Protein 2/genetics/metabolism
MH  - Lysosomes/metabolism
MH  - Male
MH  - Mice
MH  - Molecular Chaperones/*metabolism
MH  - Multiprotein Complexes
MH  - NIH 3T3 Cells
MH  - Nerve Tissue Proteins/metabolism
MH  - Peptide Elongation Factor 1/metabolism
MH  - Protein Transport
MH  - RNA Interference
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Time Factors
MH  - Transfection
PMC - PMC2945256
MID - NIHMS230167
EDAT- 2010/08/28 06:00
MHDA- 2010/09/21 06:00
PMCR- 2011/08/27
CRDT- 2010/08/28 06:00
PHST- 2009/08/19 00:00 [received]
PHST- 2010/03/07 00:00 [revised]
PHST- 2010/06/02 00:00 [accepted]
PHST- 2010/08/28 06:00 [entrez]
PHST- 2010/08/28 06:00 [pubmed]
PHST- 2010/09/21 06:00 [medline]
PHST- 2011/08/27 00:00 [pmc-release]
AID - S1097-2765(10)00614-3 [pii]
AID - 10.1016/j.molcel.2010.08.004 [doi]
PST - ppublish
SO  - Mol Cell. 2010 Aug 27;39(4):535-47. doi: 10.1016/j.molcel.2010.08.004.