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International Journal of Cell Biology
Volume 2011, Article ID 713435, 7 pages
Review Article

Atg14: A Key Player in Orchestrating Autophagy

1Faculty of Pharmaceutical Sciences, Hokkaido University, Kita-12 Jo Nishi-6 Chome, Kitaku, Sapporo 060-0812, Japan
2Frontier Research Center, Tokyo Institute of Technology, 4259-S2-12 Nagatsuda-Cho, Midoriku, Yokohama 226-8503, Japan

Received 30 May 2011; Accepted 28 July 2011

Academic Editor: Liza Pon

Copyright © 2011 Keisuke Obara and Yoshinori Ohsumi. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Phosphorylation of phosphatidylinositol (PtdIns) by a PtdIns 3-kinase is an essential process in autophagy. Atg14, a specific subunit of one of the PtdIns 3-kinase complexes, targets the complex to the probable site of autophagosome formation, thereby, sorting the complex to function specifically in autophagy. The N-terminal half of Atg14, containing coiled-coil domains, is required to form the PtdIns 3-kinase complex and target it to the proper site. The C-terminal half of yeast Atg14 is suggested to be involved in the formation of a normal-sized autophagosome. The C-terminal half of mammalian Atg14 contains the Barkor/Atg14(L) autophagosome-targeting sequence (BATS) domain that preferentially binds to the highly curved membranes containing PtdIns(3)P and is proposed to target the PtdIns 3-kinase complex efficiently to the isolation membrane. Thus, the N- and C-terminal halves of Atg14 are likely to have an essential core function and a regulatory role, respectively.