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MBC in Press, published online ahead of print January 18, 2006
Mol. Biol. Cell 10.1091/mbc.E05-09-0841

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Submitted on September 7, 2005
Revised on December 27, 2005
Accepted on January 5, 2006

Assortment of Phosphatidylinositol 3-Kinase Complexes--Atg14p Directs Association of Complex I to the Preautophagosomal Structure in Saccharomyces cerevisiae

Keisuke Obara, Takayuki Sekito, and Yoshinori Ohsumi

Division of Molecular Cell Biology, National Institute for Basic Biology, Myodaiji, Okazaki 444-8585, Japan

Monitoring Editor: Jean Gruenberg

In the yeast S. cerevisiae, two similar phosphatidylinositol 3-kinase complexes (complexes I and II) function in distinct biological processes, complex I in autophagy and complex II in the vacuolar protein sorting via endosomes. Atg14p is only integrated into complex I, likely facilitating the function of complex I in autophagy. Deletion analysis of Atg14p revealed that N-terminal region containing the coiled-coil structures was essential and sufficient for autophagy. Atg14p localized to pre-autophagosomal structure (PAS) and vacuolar membranes, whereas Vps38p, a component specific to complex II, localized to endosomes and vacuolar membranes. Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. The localization of these components to the PAS was Atg14p-dependent, but not dependent on Vps38p. Conversely, localization of these proteins to endosomes required Vps38p, but not Atg14p. Vps15p, regulatory subunit of the Vps34p complexes, localized to the PAS, vacuolar membranes, and punctate structures independent of both Atg14p and Vps38p. Taken together, these results indicate that complexes I and II function in distinct biological processes by localizing to specific compartments in a manner mediated by specific components of each complex, Atg14p and Vps38p, respectively.

Address correspondence to: Yoshinori Ohsumi (yohsumi{at}nibb.ac.jp)




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