QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 19, Issue 8, 3290-3298, August 2008

This Article Full Text Full Text (PDF) Supplemental Materials All Versions of this Article: E07-12-1292v1 19/8/3290    most recent Alert me when this article is cited Alert me if a correction is posted Services Related articles in Mol. Biol. Cell Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Xie, Z. Articles by Klionsky, D. J. Search for Related Content PubMed PubMed Citation Articles by Xie, Z. Articles by Klionsky, D. J.

Atg8 Controls Phagophore Expansion during Autophagosome Formation

Zhiping Xie^*, Usha Nair^*, and Daniel J. Klionsky^*,

*Life Sciences Institute and Department of Molecular, Cellular, and Developmental Biology, and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109

Submitted January 2, 2008; Revised April 21, 2008; Accepted May 16, 2008
Monitoring Editor: Howard Riezman

InCytes from MBC

Autophagy is a potent intracellular degradation process with pivotal roles in health and disease. Atg8, a lipid-conjugated ubiquitin-like protein, is required for the formation of autophagosomes, double-membrane vesicles responsible for the delivery of cytoplasmic material to lysosomes. How and when Atg8 functions in this process, however, is not clear. Here we show that Atg8 controls the expansion of the autophagosome precursor, the phagophore, and give the first real-time, observation-based temporal dissection of the autophagosome formation process. We demonstrate that the amount of Atg8 determines the size of autophagosomes. During autophagosome biogenesis, Atg8 forms an expanding structure and later dissociates from the site of vesicle formation. On the basis of the dynamics of Atg8, we present a multistage model of autophagosome formation. This model provides a foundation for future analyses of the functions and dynamics of known autophagy-related proteins and for screening new genes.

Address correspondence to: Daniel J. Klionsky (klionsky{at}umich.edu)

Abbreviations used: ALP, alkaline phosphatase; Atg, autophagy-related; Cvt, cytoplasm to vacuole targeting; GFP, green fluorescent protein; prApe1, precursor aminopeptidase I.

Related articles in Mol. Biol. Cell:

InCytes from MBC, August 2008

Mol. Biol. Cell 2008 19: 3179. [PDF]  

This article has been cited by other articles:

				A. Huett, A. Ng, Z. Cao, P. Kuballa, M. Komatsu, M. J. Daly, D. K. Podolsky, and R. J. Xavier A Novel Hybrid Yeast-Human Network Analysis Reveals an Essential Role for FNBP1L in Antibacterial Autophagy J. Immunol., April 15, 2009; 182(8): 4917 - 4930. [Abstract] [Full Text] [PDF]

				Y.-Y. Chang and T. P. Neufeld An Atg1/Atg13 Complex with Multiple Roles in TOR-mediated Autophagy Regulation Mol. Biol. Cell, April 1, 2009; 20(7): 2004 - 2014. [Abstract] [Full Text] [PDF]

				C. He, M. Baba, Y. Cao, and D. J. Klionsky Self-Interaction Is Critical for Atg9 Transport and Function at the Phagophore Assembly Site during Autophagy Mol. Biol. Cell, December 1, 2008; 19(12): 5506 - 5516. [Abstract] [Full Text] [PDF]

				N. Fujita, M. Hayashi-Nishino, H. Fukumoto, H. Omori, A. Yamamoto, T. Noda, and T. Yoshimori An Atg4B Mutant Hampers the Lipidation of LC3 Paralogues and Causes Defects in Autophagosome Closure Mol. Biol. Cell, November 1, 2008; 19(11): 4651 - 4659. [Abstract] [Full Text] [PDF]

				J. Geng, M. Baba, U. Nair, and D. J. Klionsky Quantitative analysis of autophagy-related protein stoichiometry by fluorescence microscopy J. Cell Biol., October 23, 2008; 182(1): 129 - 140. [Abstract] [Full Text] [PDF]

				W.-L. Yen and D. J. Klionsky How to Live Long and Prosper: Autophagy, Mitochondria, and Aging Physiology, October 1, 2008; 23(5): 248 - 262. [Abstract] [Full Text] [PDF]