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Statements

Subject Item
dbr:Chaperone-assisted_selective_autophagy
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Chaperone-assisted selective autophagy
rdfs:comment
Chaperone-assisted selective autophagy is a cellular process for the selective, ubiquitin-dependent degradation of chaperone-bound proteins in lysosomes. Autophagy (Greek: ‘self-eating’) was initially identified as a catabolic process for the unselective degradation of cellular content in lysosomes under starvation conditions. However, autophagy also comprises selective degradation pathways, which depend on ubiquitin conjugation to initiate sorting to lysosomes. In the case of chaperone-assisted selective autophagy, dysfunctional, nonnative proteins are recognized by molecular chaperones and become ubiquitinated by chaperone-associated ubiquitin ligases. The ubiquitinated proteins are enclosed in autophagosomes, which eventually fuse with lysosomes, leading to the degradation of the dysfun
dcterms:subject
dbc:Cell_biology
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38705478
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1032267499
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dbr:Proteins dbr:Muscle_dystrophy dbr:Ubiquitination dbc:Cell_biology dbr:Neurons dbr:VPS18 dbr:Lysosomes dbr:Autophagy dbr:HSPB8 dbr:STUB1 dbr:BAG3 dbr:Chaperone_(protein) dbr:Huntington's_disease dbr:Filamin dbr:HSPA8 dbr:Lung dbr:Proteostasis dbr:Huntingtin dbr:SYNPO2 dbr:Cardiomyopathy dbr:Heart dbr:Actin dbr:Skeletal_muscle dbr:SQSTM1 dbr:Ubiquitin
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Chaperone-assisted selective autophagy is a cellular process for the selective, ubiquitin-dependent degradation of chaperone-bound proteins in lysosomes. Autophagy (Greek: ‘self-eating’) was initially identified as a catabolic process for the unselective degradation of cellular content in lysosomes under starvation conditions. However, autophagy also comprises selective degradation pathways, which depend on ubiquitin conjugation to initiate sorting to lysosomes. In the case of chaperone-assisted selective autophagy, dysfunctional, nonnative proteins are recognized by molecular chaperones and become ubiquitinated by chaperone-associated ubiquitin ligases. The ubiquitinated proteins are enclosed in autophagosomes, which eventually fuse with lysosomes, leading to the degradation of the dysfunctional proteins. Chaperone-assisted selective autophagy is a vital part of the cellular protein quality control system. It is essential for protein homeostasis (proteostasis) in neurons and in mechanically strained cells and tissues such as skeletal muscle, heart and lung.
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