The Ubi brothers reunited
Open accessAbstract
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.
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Prior to fusion of autophagosomes with lysosomes, LC3-II on the outer autophagosomal membrane is released by deconjugation of PE from LC3 by Atg4, while LC3-II associated with the inner membrane is retained and eventually degraded by acid hydrolases within the autophagolysosome.
“Prior to the fusion of autophagosomes with lysosomes, the LC3-II located on the outer autophagosomal membrane is released by deconjugation of PE from LC3 by the proteolytic activity of Atg4. By contrast, LC3-II associated with the inner membrane is retained, although eventually degraded by the acid hydrolases within the autophagolysosome [27].”
From LC3-Associated Phagocytosis (LAP): Connections with Host Autophagy (2012) · cites this paper as [27]
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- 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. · DOI
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- Authors
- Noda, T., Fujita, N., & Yoshimori, T.
- Affiliations
- Research Institute for Microbial Diseases, The University of Osaka (JP)
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2008-05-16
- Volume
- 4
- Issue
- 4
- Pages
- 540-541
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- OpenAlex
- W2334805732
- Cited by
- 23
- References
- 0
- Citations by year
- 2025: 2 · 2023: 1 · 2020: 1 · 2016: 3 · 2015: 2 · 2014: 1 · 2013: 3 · 2012: 3
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Autophagy (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- ATG12, ubiquitin-like proteins, autophagosome formation, LC3 lipidation, ATG12-ATG5 conjugate
- MeSH terms
- Autophagy-Related Proteins, Autophagy-Related Protein 12, Animals, Autophagy, Carrier Proteins, Humans, Microtubule-Associated Proteins, Phagosomes, Signal Transduction, Ubiquitin, Small Ubiquitin-Related Modifier Proteins, Multiprotein Complexes
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