A ubiquitin-like system mediates protein lipidation

By Yoshinobu Ichimura, T. Kirisako, Toshifumi Takao, Y. Satomi, Y. Shimonishi, Naotada Ishihara, N. Mizushima, I. Tanida, E. Kominami, M. Ohsumi and 2 more. Nature, 2000

2,062 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology

View Paper: https://www.semanticscholar.org/paper/7dc2078ddb52295c22b137a90e46807b1e019cd5

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. N. Mizushima
2. D. Klionsky
3. Beth Levine
4. I. Slaninová
5. V. Deretic
6. Guido Kroemer
7. Y. Ohsumi
8. Zhifen Yang

In Epidemiology

1. N. Mizushima
2. D. Klionsky
3. Beth Levine
4. I. Slaninová
5. Guido Kroemer
6. V. Deretic
7. Alec C. Kimmelman
8. A. Cuervo

Citations in the corpus

• Protein turnover via autophagy: implications for metabolism. (2007, background): “Atg8 (LC3 in mammals) and Atg12 are ubiquitin-like proteins.”
• An Overview of Autophagy: Morphology, Mechanism, and Regulation (2014, background): “In yeast macroautophagy, induction of autophagosome formation is regulated by the Atg1-Atg13-Atg17Atg31-Atg29 kinase complex (43).”
• Leaf Senescence and Starvation-Induced Chlorosis Are Accelerated by the Disruption of an Arabidopsis Autophagy Gene1 (2002, background): “Apg8p is then activated by Apg7p and is subsequently attached to Apg3p, another E2-like enzyme, after which the C-terminal Gly of Apg8p is conjugated to phosphatidylethanolamine by an amide bond (Ichimura et al., 2000; Kirisako et al., 2000).”
• LC3 conjugation system in mammalian autophagy (2004, background): “In the yeastS. cerevisiae, Atg4, a cysteine protease, is essential for the cleavage of the carboxyl terminus of Atg8 to expose Gly (Ichimura et al., 2000).”
• Autophagy: molecular machinery for self-eating (2005, background): “The other conjugation system involves Atg8 as a modifier of a lipid, phosphatidylethanolamine.(59,60) Atg8 was originally characterized as a microtubule-associated protein required for autophagy and the Cvt pathway,(61) although a functional association with microtubules has not been substantiated.”
• LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation (2004, background): “The exposed Gly of Atg8 is conjugated to phosphatidylethanolamine (PE), which is catalysed by Atg7 (an E1-like enzyme) and Atg3 (an E2-like enzyme) (Ichimura et al., 2000).”
• Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. (2007, background): “The microtubule-associated protein 1A/1B light chain 3 (LC3) is a modifier protein conjugated with phosphatidylethanolamine (PE), analogous to Atg8 in yeast (Ichimura et al., 2000).”
• The molecular machinery of autophagy: unanswered questions (2005, background): “Atg8 is a Ubl Journal of Cell Science 118 (1) Jo ur na l o f C el l S ci en ce that undergoes proteolytic processing by the Atg4 protease to reveal a glycine residue that is then covalently attached to PE (Ichimura et al., 2000).”
• Hierarchy of Atg proteins in pre‐autophagosomal structure organization (2007, background): “Our previous works showed that an ubiquitin-like conjugation system attaches Atg8p to phosphatidylethanolamine (PE) (Ichimura et al. 2000).”
• Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice (2005, background): “It is generally accepted that LC3-I is the free mature form whereas LC3-II is the lipidated form, in analogy to yeast Atg8p (Ichimura et al., 2000; Kabeya et al., 2000).”
• Autophagy regulates programmed cell death during the plant innate immune response. (2005, background): “Two proteins of the conjugation athways required for autophagy are Atg7 and Atg3 Ichimura et al., 2000).”