Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print December 27, 2006
Mol. Biol. Cell 10.1091/mbc.E06-08-0683

A more recent version of this article appeared on March 1, 2007
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E06-08-0683v1
18/3/919    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chang, C.-Y.
Right arrow Articles by Huang, W.-P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chang, C.-Y.
Right arrow Articles by Huang, W.-P.

Submitted on August 7, 2006
Revised on November 27, 2006
Accepted on December 20, 2006

Atg19 Mediates a Dual Interaction Cargo Sorting Mechanism in Selective Autophagy

Chiung-Ying Chang* and Wei-Pang Huang*{dagger}

*Institute of Zoology and {dagger}Department of Life Science, National Taiwan University, Taipei 106, Taiwan, Republic of China

Monitoring Editor: Suresh Subramani

Autophagy is a catabolic membrane trafficking mechanism conserved in all eukaryotic cells. In addition to the nonselective transport of bulk cytosol, autophagy is responsible for efficient delivery of the vacuolar enzyme Ape1 precursor (prApe1) in the budding yeast S. cerevisiae, suggesting the presence of a prApe1 sorting machinery. Sequential interactions between Atg19-Atg11 and Atg19-Atg8 pairs are thought responsible for targeting prApe1 to the vesicle formation site, the pre-autophagosomal structure (PAS), and loading it into transport vesicles, respectively. However, the different patterns of prApe1 transport defect seen in the atg11{Delta} and atg19{Delta} strains seem to be incompatible with this model. Here we report that prApe1 could not be targeted to the PAS and failed to be delivered into the vacuole in atg8{Delta} atg11{Delta} double knockout cells regardless of the nutrient conditions. We postulate that Atg19 mediates a dual interaction prApe1 sorting mechanism through independent, instead of sequential, interactions with Atg11 and Atg8. In addition, to efficiently deliver prApe1 to the vacuole, a proper interaction between Atg11 and Atg9 is indispensable. We speculate that Atg11 may elicit a cargo-loading signal and induce Atg9 shuttling to specific PAS site, where Atg9 relays the signal and recruits other Atg proteins to induce vesicle formation.

Address correspondence to: Wei-Pang Huang (wphuang{at}ntu.edu.tw)






Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2006 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.