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Originally published In Press as doi:10.1074/jbc.M802403200 on September 25, 2008
J. Biol. Chem., Vol. 283, Issue 47, 32386-32393, November 21, 2008
Mitophagy in Yeast Occurs through a Selective Mechanism*
Tomotake Kanki and
Daniel J. Klionsky1
From the
Life Sciences Institute and Departments of Molecular, Cellular, and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109
The regulation of mitochondrial degradation through autophagy is expected to be a tightly controlled process, considering the significant role of this organelle in many processes ranging from energy production to cell death. However, very little is known about the specific nature of the degradation process. We developed a new method to detect mitochondrial autophagy (mitophagy) by fusing the green fluorescent protein at the C terminus of two endogenous mitochondrial proteins and monitored vacuolar release of green fluorescent protein. Using this method, we screened several atg mutants and found that ATG11, a gene that is essential only for selective autophagy, is also essential for mitophagy. In addition, we found that mitophagy is blocked even under severe starvation conditions, if the carbon source makes mitochondria essential for metabolism. These findings suggest that the degradation of mitochondria is a tightly regulated process and that these organelles are largely protected from nonspecific autophagic degradation.
Received for publication, March 27, 2008
, and in revised form, September 10, 2008.
* This work was supported, in whole or in part, by National Institutes of Health Grant GM53396 (to D. J. K.). This work was also supported by Japan Society for the Promotion of Science Postdoctoral Fellowships for Research Abroad (to T. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1–S3.
1 To whom correspondence should be addressed: Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109-2216. Tel.: 734-615-6556; Fax: 734-763-6492; E-mail: klionsky{at}umich.edu.

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Copyright © 2008 by the American Society for Biochemistry and Molecular Biology.
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