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EMBO J. 1999 Jul 15;18(14):3888-96.

Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.

Author information

1
Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan.

Abstract

Autophagy is an intracellular bulk degradation system that is ubiquitous for eukaryotic cells. In this process, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. We recently found that a protein conjugation system, in which Apg12p is covalently attached to Apg5p, is indispensable for autophagy in yeast. Here, we describe a novel coiled-coil protein, Apg16p, essential for autophagy. Apg16p interacts with Apg12p-conjugated Apg5p and less preferentially with unconjugated Apg5p. Moreover, the coiled-coil domain of Apg16p mediates self-multimerization that leads to cross-linking of Apg5p molecules and formation of a stable protein complex. Apg16p is not essential for the Apg12p-Apg5p conjugation reaction. These results suggest that the Apg12p-Apg5p conjugate requires Apg16p to accomplish its role in the autophagy pathway, and Apg16p is a key molecule as a linker to form the Apg12p-Apg5p-Apg16p multimer.

PMID:
10406794
PMCID:
PMC1171465
DOI:
10.1093/emboj/18.14.3888
[Indexed for MEDLINE]
Free PMC Article
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