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J. Biol. Chem., Vol. 278, Issue 20, 17636-17645, May 16, 2003
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From the Macroautophagy is a mechanism employed by
eukaryotic cells to recycle non-essential cellular components during
starvation, differentiation, and development. Two conjugation reactions
related to ubiquitination are essential for autophagy: Apg12p
conjugation to Apg5p, and Apg8p conjugation to the lipid
phosphatidylethanolamine. These reactions require the action of the
E1-like enzyme, Apg7p, and the E2-like enzymes, Apg3p and Apg10p. In
Dictyostelium, development is induced by starvation,
conditions under which autophagy is required for survival in yeast and
plants. We have identified Dictyostelium homologues of 10 budding yeast autophagy genes. We have generated mutations in
apg5 and apg7 that produce defects typically
associated with an abrogation of autophagy. Mutants are not grossly
affected in growth, but survival during nitrogen starvation is severely
reduced. Starved mutant cells show little turnover of cellular
constituents by electron microscopy, whereas wild-type cells show
significant cytoplasmic degradation and reduced organelle number. Bulk
protein degradation during starvation-induced development is reduced in
the autophagy mutants. Development is aberrant; the autophagy mutants
do not aggregate in plaques on bacterial lawns, but they do proceed
further in development on nitrocellulose filters, forming defective
fruiting bodies. The autophagy mutations are cell autonomous, because
wild-type cells in a chimaera do not rescue development of the
autophagy mutants. We have complemented the mutant phenotypes by
expression of the cognate gene fused to green fluorescent protein. A
green fluorescent protein fusion of the autophagosome marker
Apg8 mislocalizes in the two autophagy mutants. We show that the
Apg5-Apg12 conjugation system is conserved in
Dictyostelium.
Macroautophagy Is Required for Multicellular Development of the
Social Amoeba Dictyostelium discoideum*
,,,¶
Department of Anatomy and Cell Biology,
Columbia University, New York, New York 10032 and
§ Department of Biology, Lamont-Doherty Earth Observatory,
Columbia University, Palisades, New York 10964
*
This work was supported in part by National Institutes of
Health Grant GM33136 (to R. H. K.). This is Lamont-Doherty Earth Observatory Contribution Number 6408.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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