![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
|
|
|
|
|
||
A more recent version of this article appeared on November 1, 2008
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on March 25, 2008
Revised on July 9, 2008
Accepted on August 26, 2008
*Department of Cellular Regulation, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan; Department of Genetics, The Graduate University for Advanced Studies, Mishima 455-8540, Japan; Department of Cell Biology, Nagahama Institute of Bio-Science and Technology, Nagahama, Shiga 526-0829, Japan; CREST, Japan Science and Technology Agency, Kawaguchi-Saitama 332-0012, Japan
Monitoring Editor: Suresh Subramani
In the process of autophagy, a ubiquitin-like molecule, LC3/Atg8, is conjugated to phosphatidylethanolamine (PE) and associates with forming autophagosomes. In mammalian cells, the existence of multiple Atg8 homologues (referred to as LC3 paralogues) has hampered genetic analysis of the lipidation of LC3 paralogues. Here, we show that overexpression of an inactive mutant of Atg4B, a protease that processes proLC3 paralogues, inhibits autophagic degradation and lipidation of LC3 paralogues. Inhibition was caused by sequestration of free LC3 paralogues in stable complexes with the Atg4B mutant. In mutant overexpressing cells, Atg5- and ULK1-positive intermediate autophagic structures accumulated. The length of these membrane structures was comparable to that in control cells; however, a significant number were not closed. These results show that the lipidation of LC3 paralogues is involved in the completion of autophagosome formation in mammalian cells. This study also provides a powerful tool for a wide variety of studies of autophagy in the future.
This article has been cited by other articles:
|
|
 |
|
  C. Kubota, S. Torii, N. Hou, N. Saito, Y. Yoshimoto, H. Imai, and T. Takeuchi Constitutive Reactive Oxygen Species Generation from Autophagosome/Lysosome in Neuronal Oxidative Toxicity J. Biol. Chem., January 1, 2010; 285(1): 667 - 674. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Fujita, T. Saitoh, S. Kageyama, S. Akira, T. Noda, and T. Yoshimori Differential Involvement of Atg16L1 in Crohn Disease and Canonical Autophagy: ANALYSIS OF THE ORGANIZATION OF THE Atg16L1 COMPLEX IN FIBROBLASTS J. Biol. Chem., November 20, 2009; 284(47): 32602 - 32609. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Noda and T. Yoshimori Molecular basis of canonical and bactericidal autophagy Int. Immunol., November 1, 2009; 21(11): 1199 - 1204. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Simonsen and S. A. Tooze Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes J. Cell Biol., September 21, 2009; 186(6): 773 - 782. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Dreux, P. Gastaminza, S. F. Wieland, and F. V. Chisari The autophagy machinery is required to initiate hepatitis C virus replication PNAS, August 18, 2009; 106(33): 14046 - 14051. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 V. M. S. Betin and J. D. Lane Caspase cleavage of Atg4D stimulates GABARAP-L1 processing and triggers mitochondrial targeting and apoptosis J. Cell Sci., July 15, 2009; 122(14): 2554 - 2566. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Ishida, A. Yamamoto, A. Kitamura, S. R. Lamande, T. Yoshimori, J. F. Bateman, H. Kubota, and K. Nagata Autophagic Elimination of Misfolded Procollagen Aggregates in the Endoplasmic Reticulum as a Means of Cell Protection Mol. Biol. Cell, June 1, 2009; 20(11): 2744 - 2754. [Abstract] [Full Text] [PDF]
|
|
