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Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins.
- Source :
-
Nature structural & molecular biology [Nat Struct Mol Biol] 2014 Apr; Vol. 21 (4), pp. 336-45. - Publication Year :
- 2014
-
Abstract
- Autophagy complements the ubiquitin-proteasome system in mediating protein turnover. Whereas the proteasome degrades individual proteins modified with ubiquitin chains, autophagy degrades many proteins and organelles en masse. Macromolecules destined for autophagic degradation are 'selected' through sequestration within a specialized double-membrane compartment termed the phagophore, the precursor to an autophagosome, and then are hydrolyzed in a lysosome- or vacuole-dependent manner. Notably, a pair of distinctive ubiquitin-like proteins (UBLs), Atg8 and Atg12, regulate degradation by autophagy in unique ways by controlling autophagosome biogenesis and recruitment of specific cargos during selective autophagy. Here we review structural mechanisms underlying the functions and conjugation of these UBLs that are specialized to provide interaction platforms linked to phagophore membranes.
- Subjects :
- Adaptor Proteins, Signal Transducing chemistry
Adaptor Proteins, Signal Transducing metabolism
Adaptor Proteins, Signal Transducing physiology
Autophagy-Related Protein 8 Family
Autophagy-Related Proteins
Cysteine Endopeptidases metabolism
Cysteine Endopeptidases physiology
Humans
Microfilament Proteins chemistry
Microfilament Proteins metabolism
Microfilament Proteins physiology
Models, Biological
Proteasome Endopeptidase Complex physiology
Proteolysis
Ubiquitins chemistry
Ubiquitins metabolism
Autophagy physiology
Ubiquitins physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1545-9985
- Volume :
- 21
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Nature structural & molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 24699082
- Full Text :
- https://doi.org/10.1038/nsmb.2787