Recommend Autophagy to your librarian for 2008. Download form here.

Sign up for Table of Contents Alerts!

home subscribe search archive forthcoming

Email this page Print this page

Article Addendum

The Ubi brothers reunited

Takeshi Noda, Naonobu Fujita and Tamotsu Yoshimori

volume 4 | issue 4

16 May 2008
Pages: 540 - 541

Purchase article for $19

Subscribe to this journal for $99/year

Atg12 and Atg8/LC3 are two ubiquitin-like proteins involved in autophagosome formation. They show several similar characteristics just like brothers evolved from the same ancestor, however, their functional relationship has been obscure. We recently reported that a super protein complex, the Atg16L complex, which consists of multiple Atg12-Atg5 conjugates and the associating protein Atg16L, has an E3-like role in the LC3 lipidation reaction 1. The activated intermediate, LC3-Atg3 (E2) is recruited to the site where the lipidation takes place by virtue of the Atg16L complex. Thus, these two closely resembling systems are connected also in terms of their functions. This finding will provide further important clues as to the origin of the autophagosome membrane, and how the process is regulated by starvation and PtdIns3P signals.

Addendum to: Fujita N, Itoh T, Fukuda M, Noda T, Yoshimori T. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol Biol Cell 2008:10.1091/mbc.E07-12-257.

Authors

Takeshi Noda

Osaka University

Naonobu Fujita

Osaka University

Tamotsu Yoshimori

Osaka University


Purchase article for $19

Subscribe to this journal for $99/year