The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex–dependent and –independent autophagy
Open accessAbstract
Autophagy is a finely orchestrated cellular catabolic process that requires multiple autophagy-related gene products (ATG proteins). The ULK1 complex functions to integrate upstream signals to downstream ATG proteins through an unknown mechanism. Here we have identified an interaction between mammalian FIP200 and ATG16L1, essential components of the ULK1 and ATG5 complexes, respectively. Further analyses show this is a direct interaction mediated by a short domain of ATG16L1 that we term the FIP200-binding domain (FBD). The FBD is not required for ATG16L1 self-dimerization or interaction with ATG5. Notably, an FBD-deleted ATG16L1 mutant is defective in mediating amino acid starvation–induced autophagy, which requires the ULK1 complex. However, this mutant retains its function in supporting glucose deprivation–induced autophagy, a ULK1 complex–independent process. This study therefore identifies a previously uncharacterized interaction between the ULK1 and ATG5 complexes that can distinguish ULK1-dependent and -independent autophagy processes.
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1 retracted
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RetractedAutophagy in the Pathogenesis of Disease
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Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice
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ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
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Beclin 1 Forms Two Distinct Phosphatidylinositol 3-Kinase Complexes with Mammalian Atg14 and UVRAG
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The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy
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Cited by
The mammalian ULK1 complex and autophagy initiation
Zachari, M., & Ganley, I. G. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170021 · Cited by 789
Autophagy regulation by nutrient signaling
Russell, R. C., Yuan, H.-X., & Guan, K.-L. (2014) · Cell Research · doi:10.1038/cr.2013.166 · Cited by 710
Galectin-3 Coordinates a Cellular System for Lysosomal Repair and Removal
Jia, J., Claude-Taupin, A., Gu, Y., Choi, S. W., Peters, R., Bissa, B., Mudd, M. H., Allers, L., Pallikkuth, S., Lidke, K. A., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2019.10.025 · Cited by 434
Smith, M. D., Harley, M. E., Kemp, A. J., Wills, J., Lee, M., Arends, M., von Kriegsheim, A., Behrends, C., & Wilkinson, S. (2018) · Developmental Cell · doi:10.1016/j.devcel.2017.11.024 · Cited by 444
Autophagy initiation by ULK complex assembly on ER tubulovesicular regions marked by ATG9 vesicles
Karanasios, E., Walker, S. A., Okkenhaug, H., Manifava, M., Hummel, E., Zimmermann, H., Ahmed, Q., Domart, M.-C., Collinson, L., & Ktistakis, N. T. (2016) · Nature Communications · doi:10.1038/ncomms12420 · Cited by 321
Metadata
- Authors
- Gammoh, N., Florey, O., Overholtzer, M., & Jiang, X.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2012-12-23
- Volume
- 20
- Issue
- 2
- Pages
- 144-149
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2171520517
- Cited by
- 208
- References
- 13
- FWCI
- 7.76
- Type
- journal article
- Language
- en
- Open access
- green
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- Gammoh, N., Florey, O., Overholtzer, M., & Jiang, X. (2013). Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex–dependent and –independent autophagy. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.2475
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