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Identification of regulators of chaperone-mediated autophagy.

Authors: Bandyopadhyay, U  Sridhar, S  Kaushik, S  Kiffin, R  Cuervo, AM 
Citation: Bandyopadhyay U, etal., Mol Cell. 2010 Aug 27;39(4):535-47. doi: 10.1016/j.molcel.2010.08.004.
Pubmed: (View Article at PubMed) PMID:20797626
DOI: Full-text: DOI:10.1016/j.molcel.2010.08.004

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.


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CRRD Object Information
CRRD ID: 10412296
Created: 2015-11-14
Species: All species
Last Modified: 2015-11-14
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.