Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast.
Autophagy, responsible for the delivery of cytoplasmic components to the lysosome/vacuole for degradation, is the major degradative pathway in eukaryotic cells. This process requires a ubiquitin-like protein conjugation system, in which Apg12 is covalently bound to Apg5. In the yeast Saccharomyces cerevisiae, the Apg12-Apg5 conjugate further interacts with a small ... coiled-coil protein, Apg16. The Apg12-Apg5 and Apg16 are localized in the cytosol and pre-autophagosomal structures and play an essential role in autophagosome formation. Here we show that the Apg12-Apg5 conjugate and Apg16 form a approximately 350-kDa complex in the cytosol. Because Apg16 was suggested to form a homo-oligomer, we generated an in vivo system that allowed us to control the oligomerization state of Apg16. With this system, we demonstrated that formation of the approximately 350-kDa complex and autophagic activity depended on the oligomerization state of Apg16. These results suggest that the Apg12-Apg5 conjugate and Apg16 form a multimeric complex mediated by the Apg16 homo-oligomer, and formation of the approximately 350-kDa complex is required for autophagy in yeast.
Mesh Terms:
Autophagy, Base Sequence, Carrier Proteins, Chromatography, Gel, Cytosol, DNA Primers, Membrane Proteins, Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors
Autophagy, Base Sequence, Carrier Proteins, Chromatography, Gel, Cytosol, DNA Primers, Membrane Proteins, Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors
J. Biol. Chem.
Date: May. 24, 2002
PubMed ID: 11897782
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