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Vol. 12, Issue 11, 3690-3702, November 2001
*Department of Cell Biology, National Institute for Basic Biology,
The Graduate University for Advanced Studies, Okazaki, 444-8585, Japan;
and §Biological Program, Yamanashi Medical University,
Yamanashi, 409-3898, Japan
Double membrane structure, autophagosome, is formed de
novo in the process of autophagy in the yeast
Saccharomyces cerevisiae, and many Apg proteins
participate in this process. To further understand autophagy, we
analyzed the involvement of factors engaged in the secretory pathway.
First, we showed that Sec18p (N-ethylmaleimide-sensitive fusion protein, NSF) and Vti1p (soluble
N-ethylmaleimide-sensitive fusion protein attachment
protein, SNARE), and soluble N-ethylmaleimide-sensitive fusion protein receptor are required for fusion of the autophagosome to
the vacuole but are not involved in autophagosome formation. Second,
Sec12p was shown to be essential for autophagy but not for the
cytoplasm to vacuole-targeting (Cvt) (pathway, which shares mostly the
same machinery with autophagy. Subcellular fractionation and electron
microscopic analyses showed that Cvt vesicles, but not autophagosomes,
can be formed in sec12 cells. Three other coatmer
protein (COPII) mutants, sec16, sec23,
and sec24, were also defective in autophagy. The
blockage of autophagy in these mutants was not dependent on transport
from endoplasmic reticulum-to-Golgi, because mutations in two other
COPII genes, SEC13 and SEC31, did not
affect autophagy. These results demonstrate the requirement for
subgroup of COPII proteins in autophagy. This evidence demonstrating the involvement of Sec proteins in the mechanism of autophagosome formation is crucial for understanding membrane flow during the process.
These authors contributed equally to this work.
Present address: Department of Molecular
Biology, Graduate School of Medical Science, Kyushu University,
Fukuoka, 812-8582, Japan.
Corresponding author. E-mail address: yohsumi{at}nibb.ac.jp.
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