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. 1999 Jul 15;18(14):3888-96.
doi: 10.1093/emboj/18.14.3888.

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

N Mizushima  1 , T Noda, Y Ohsumi
Affiliations

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

N Mizushima et al. EMBO J. .

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.

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