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Article Addendum
Atg9 Trafficking in Autophagy-Related Pathways
Congcong He and Daniel J. Klionsky
volume 3 | issue 3
May/June 2007Pages: 271 - 274
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The origin of the autophagosomal membrane and the lipid delivery mechanism during autophagy remain unsolved mysteries. Some important hints to these questions come from Atg9, which is the only integral membrane protein required for autophagosome formation and considered a membrane carrier in autophagy-related pathways. In S. cerevisiae, Atg9 cycles between peripheral sites and the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle. We recently identified a peripheral membrane protein, Atg11, as a binding partner of Atg9, in a yeast two-hybrid screen. Based on our analysis we propose a model for Atg9 cycling. Our model suggests that a pool of Atg11 mediates the anterograde transport of Atg9 to the PAS along the actin cytoskeleton, and that this delivery process may serve as a membrane shuttle for vesicle assembly during yeast selective autophagy. Here, we discuss the implications of the model and present additional evidence that extends it with regard to membrane trafficking modes during pexophagy.
Addendum to:
Recruitment of Atg9 to the Preautophagosomal Structure by Atg11 is Essential for Selective Autophagy in Budding Yeast
C. He, H. Song, T. Yorimitsu, I. Monastyrska, W.-L. Yen, J.E. Legakis and D.J. Klionsky
J Cell Biol 2006; 175:925-35
Authors
Congcong He
University of Michigan
Daniel J. Klionsky
Life Sciences Institute and Department of Molecular, Cellular and Developmental Biology, and Department of Biological Chemistry; University of Michigan; Ann Arbor, Michigan USA
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.