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Chaperone-mediated autophagy dysfunction in the pathogenesis of neurodegeneration

Chaperone-mediated autophagy dysfunction in the pathogenesis of neurodegeneration,10.1016/j.nbd.2010.07.006,Neurobiology of Disease,Hiroshi Koga,Ana M

Chaperone-mediated autophagy dysfunction in the pathogenesis of neurodegeneration   (Citations: 3)
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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.”
Journal: Neurobiology of Disease - NEUROBIOL DISEASE , vol. 43, no. 1, pp. 29-37, 2011
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    • ...In contrast to the vesicle-mediated substrate delivery of macro and microautophagy, chaperone-mediated autophagy (CMA) targets and delivers substrate proteins directly across the lysosomal membrane via the specific receptor [9, 12]...
    • ...This CMA substrate-chaperone complex locates to the lysosome through interaction with the lysosome receptor and translocates the substrate across the lysosomal membrane with the assistance of lysosomal chaperones on the lumenal side [12, 13]...
    • ... acidic protein (GFAP), a component of the intermediate filament network, associates to Lamp2a once it is organized into multimers and contributes to stabilizing the CMA translocation complex against the disassembling activity of Hsc70, whereas GTP-mediated release of elongation factor-1a from the lysosomal membrane promotes self-association of GFAP, disassembly of the CMA translocation complex and the consequent decrease in CMA [12, 64]...
    • ...Increasing evidence suggests that CMA acts as a cell protector and its dysfunction is correlated with diverse pathologies [3, 12]...

    Wenming Liet al. Chaperone-mediated autophagy: machinery, regulation and biological con...

    • ...]. Both CMA and macroautophagy are upregulated by nutrient deprivation [...

    Marie-Pierre Hinaultet al. Molecular Chaperones and Associated Cellular Clearance Mechanisms agai...

    • ...However, the selective clearance of cytosolic proteins via chaperone-mediated autophagy is low under basal conditions in most cells but is maximally activated in response to stress (Koga and Cuervo 2010)...
    • ...Evidence has suggested that the crosstalk between macroautophagy and chaperone-mediated autophagy operates bi-directionally to ensure that deficiency in one pathway triggers compensatory activation of the other (Kaushik et al. 2008; Koga and Cuervo 2010)...

    Virawudh Soontornniyomkijet al. Increased hippocampal accumulation of autophagosomes predicts short-te...

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