The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
The Atg8 family: multifunctional ubiquitin-like key regulators of autophagy
Abstract
Autophagy is an evolutionarily-conserved catabolic process initiated by the engulfment of cytosolic components in a crescent-shaped structure, called the phagophore, that expands and fuses to form a closed double-membrane vesicle, the autophagosome. Autophagosomes are subsequently targeted to the lysosome/vacuole with which they fuse to degrade their content. The formation of the autophagosome is carried out by a set of autophagy-related proteins (Atg), highly conserved from yeast to mammals. The Atg8s are Ubl (ubiquitin-like) proteins that play an essential role in autophagosome biogenesis. This family of proteins comprises a single member in yeast and several mammalian homologues grouped into three subfamilies: LC3 (light-chain 3), GABARAP (γ-aminobutyric acid receptor-associated protein) and GATE-16 (Golgi-associated ATPase enhancer of 16 kDa). The Atg8s are synthesized as cytosolic precursors, but can undergo a series of post-translational modifications leading to their tight association with autophagosomal structures following autophagy induction. Owing to this feature, the Atg8 proteins have been widely served as key molecules to monitor autophagosomes and autophagic activity. Studies in both yeast and mammalian systems have demonstrated that Atg8s play a dual role in the autophagosome formation process, coupling between selective incorporation of autophagy cargo and promoting autophagosome membrane expansion and closure. The membrane-remodelling activity of the Atg8 proteins is associated with their capacity to promote tethering and hemifusion of liposomes in vitro.
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Citations
Cites
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
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Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy
Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996
Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
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Self-citationReactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
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Self-citationThe Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy
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“It has been shown that the localization of the Atg12–Atg5–Atg16 complex dictates the site of Atg8 lipidation and facilitates the lipidation reaction by promoting the transfer of Atg8 from Atg3 to PE thus acting as a ubiquitin ligase (E3)-like enzyme [15].”
BackgroundFormation Process of Autophagosome Is Traced with Apg8/Aut7p in Yeast
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Ubiquitination and selective autophagy
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Self-citationAtg8: an autophagy-related ubiquitin-like protein family.
Shpilka, T., Weidberg, H., Pietrokovski, S., & Elazar, Z. (2011) · Genome biology · doi:10.1186/gb-2011-12-7-226 · Cited by 543 · cited 3×
“Humans have a single GATE-16 gene, two GABARAP genes [GABARAP and GABARAPL1 (γ-aminobutyric acid receptor-associated protein-like 1)] and four LC3 genes (LC3A, LC3B, LC3B2 and LC3C) [6].”
BackgroundInfluential
Cited by
Mechanism and medical implications of mammalian autophagy
Dikic, I., & Elazar, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0003-4 · Cited by 2,771
Self-citationCargo recognition and trafficking in selective autophagy
Stolz, A., Ernst, A., & Dikic, I. (2014) · Nature Cell Biology · doi:10.1038/ncb2979 · Cited by 1,207
p62/SQSTM 1 functions as a signaling hub and an autophagy adaptor
Katsuragi, Y., Ichimura, Y., & Komatsu, M. (2015) · The FEBS Journal · doi:10.1111/febs.13540 · Cited by 788
Ubiquitin-Dependent And Independent Signals In Selective Autophagy
Khaminets, A., Behl, C., & Dikic, I. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.08.010 · Cited by 717
E2 enzymes: more than just middle men
Stewart, M. D., Ritterhoff, T., Klevit, R. E., & Brzovic, P. S. (2016) · Cell Research · doi:10.1038/cr.2016.35 · Cited by 594
Metadata
- Authors
- Slobodkin, M. R., & Elazar, Z.
- Venue
- Essays in Biochemistry
- Publisher
- Portland Press Ltd.
- Published
- 2013-09-27
- Volume
- 55
- Pages
- 51-64
- ISSN
- 0071-1365 (ISSN-L)
- 1744-1358
- OpenAlex
- W2151950127
- Cited by
- 261
- References
- 10
- FWCI
- 11.24
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
