LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation

By Y. Kabeya, N. Mizushima, A. Yamamoto, S. Oshitani-Okamoto, Y. Ohsumi, T. Yoshimori. Journal of Cell Science, 2004

1,424 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology

View Paper: https://www.semanticscholar.org/paper/ac78497cc8877e8c3d02232d7d2d28075ab5fad0

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

In Epidemiology

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

Citations in the corpus

• Atg8 controls phagophore expansion during autophagosome formation. (2008, background): “The PAS population of Atg8 is presumably associated with the phagophore (Kirisako et al., 1999; Kabeya et al., 2000, 2004).”
• Mechanisms of Selective Autophagy (2016, neutral): “LC3C, respectively) and the three members of the gamma-aminobutyric receptorassociated protein (GABARAP) subfamily (GABARAP, GABARAP-L1 and GABARAPL2/GATE-16) [77-80].”
• ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. (2009, background): “ULK1 also interacts with GATE-16 and GABARAP, the mammalian homologues of Atg8 that localize to autophagosome (Okazaki et al., 2000; Kabeya et al., 2004).”
• Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (2012, positive): “The mammalian Atg8 homologs share from 29% to 94% sequence identity with the yeast protein and have all, apart from GABARAPL3, been demonstrated to be involved in autophagosome biogenesis.(141) The LC3 proteins are involved in phagophore formation, with participation of GABARAP subfamily members in ”
• Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria (2010, methodology): “monitored autophagy in these cells upon IL-3 deprivation, using processing of cytosolic microtubule-associated protein light chain-3 (LC3)-I into LC3-II as an autophagy-specific marker.(31,32) Consistent with a recent report,(33) IL-3 deprivation was associated with increased autophagy during the fi”
• Ubiquitination and selective autophagy (2012, background): “Among all Atg8 homologues LC3B has been extensively studied and is emerging as the main actor in starvation-induced autophagy.(50) The exact function of either LC3 or GABARAP/GATE-16 in the autophagic process remains”
• Mitochondria and Mitophagy: The Yin and Yang of Cell Death Control (2012, background): “12-ATG5, that promote assembly of the ATG16L complex and the conjugation of LC3 with phosphatidylethanolamine.(4,5) The”
• The molecular machinery of autophagy: unanswered questions (2005, background): “Whether they all play a role in autophagy is not known, although a recent study suggests that all three proteins are localized to autophagosomal membranes (Kabeya et al., 2004).”
• Autophagy and autophagy-related proteins in cancer (2020, background): “The ATG4B has been reported that it is the sole enzyme to efficiently cleave LC3 precursors and LC3-I/PE among four human homologues of yeast Atg4 (Atg4A-D) [151].”
• Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice (2005, background): “In mammals, there exist at least three Atg8 homologues that can all be activated by Atg7 (Tanida et al., 2001), GATE-16, GABARAP, and LC3 (Ohsumi, 2001), and they localize to the autophagosome (Kabeya et al., 2000, 2004).”