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Published online 18 September 2000. doi:10.1083/jcb.150.6.1507
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© The Rockefeller University Press, 0021-9525/2000//1507 $5.00
The Journal of Cell Biology, Volume 150, Number 6, , 2000 1507-1513

Report

Tor-Mediated Induction of Autophagy via an Apg1 Protein Kinase Complex



Yoshiaki Kamadaa,b, Tomoko Funakoshia, Takahiro Shintania, Kazuya Naganoc, Mariko Ohsumic, and Yoshinori Ohsumia,b

a Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan
b School of Life Science, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan
c Department of Biosciences, Teikyo University of Science and Technology, Yamanashi 409-0193, Japan
Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan.81-564-55-751681-564-55-7515

Autophagy is a membrane trafficking to vacuole/lysosome induced by nutrient starvation. In Saccharomyces cerevisiae, Tor protein, a phosphatidylinositol kinase-related kinase, is involved in the repression of autophagy induction by a largely unknown mechanism. Here, we show that the protein kinase activity of Apg1 is enhanced by starvation or rapamycin treatment. In addition, we have also found that Apg13, which binds to and activates Apg1, is hyperphosphorylated in a Tor-dependent manner, reducing its affinity to Apg1. This Apg1–Apg13 association is required for autophagy, but not for the cytoplasm-to-vacuole targeting (Cvt) pathway, another vesicular transport mechanism in which factors essential for autophagy (Apg proteins) are also employed under vegetative growth conditions. Finally, other Apg1-associating proteins, such as Apg17 and Cvt9, are shown to function specifically in autophagy or the Cvt pathway, respectively, suggesting that the Apg1 complex plays an important role in switching between two distinct vesicular transport systems in a nutrient-dependent manner.

Key Words: starvation • Cvt • yeast • rapamycin • phosphorylation

© 2000 The Rockefeller University Press

Yoshiaki Kamada and Tomoko Funakoshi contributed equally to this work.

Tomoko Funakoshi's present address is Department of Biochemistry, College of Pharmacy, Nihon University, Funabashi, Chiba 274-8555, Japan.

Abbreviations used in this paper: API, aminopeptidase I; Cvt, cytoplasm-to-vacuole targeting; HA, hemagglutinin.


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