The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
ATG8 Family Proteins Act as Scaffolds for Assembly of the ULK Complex
Open accessAbstract
Autophagy is a lysosome-dependent degradation system conserved among eukaryotes. The mammalian Atg1 homologues, Unc-51 like kinase (ULK) 1 and 2, are multifunctional proteins with roles in autophagy, neurite outgrowth, and vesicle transport. The mammalian ULK complex involved in autophagy consists of ULK1, ULK2, ATG13, FIP200, and ATG101. We have used pulldown and peptide array overlay assays to study interactions between the ULK complex and six different ATG8 family proteins. Strikingly, in addition to ULK1 and ULK2, ATG13 and FIP200 interacted with human ATG8 proteins, all with strong preference for the GABARAP subfamily. Similarly, yeast and Drosophila Atg1 interacted with their respective Atg8 proteins, demonstrating the evolutionary conservation of the interaction. Use of peptide arrays allowed precise mapping of the functional LIR motifs, and two-dimensional scans of the ULK1 and ATG13 LIR motifs revealed which substitutions that were tolerated. This information, combined with an analysis of known LIR motifs, provides us with a clearer picture of sequence requirements for LIR motifs. In addition to the known requirements of the aromatic and hydrophobic residues of the core motif, we found the interactions to depend strongly on acidic residues surrounding the central core LIR motifs. A preference for either a hydrophobic residue or an acidic residue following the aromatic residue in the LIR motif is also evident. Importantly, the LIR motif is required for starvation-induced association of ULK1 with autophagosomes. Our data suggest that ATG8 proteins act as scaffolds for assembly of the ULK complex at the phagophore.
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Cites
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
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“Moreover, acidic residues adjacent to the core motif are also important for the interactions of ULK1 and ATG13 with GABARAP, completely in line with what has been reported for the LIR motif of p62 (16).”
BackgroundInfluentialSelf-citationNutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy
Hosokawa, N., Hara, T., Kaizuka, T., Kishi, C., Takamura, A., Miura, Y., Iemura, S.-I., Natsume, T., Takehana, K., Yamada, N., et al. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1248 · Cited by 2,076
ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
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Mammalian autophagy: core molecular machinery and signaling regulation
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Network organization of the human autophagy system
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Nix is a selective autophagy receptor for mitochondrial clearance
Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2009.256 · Cited by 1,309 · cited 1×
“p62 (16), NBR1 (19), AtNBR1 (43), ATG4B (44), TP53INP1 and TP53INP2/DOR (45), FYCO1 (21), Dvl2 (46), NIX (47), FUNDC1 (48), Calreticulin (49), clathrin heavy”
Structural Basis for Sorting Mechanism of p62 in Selective Autophagy
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“C, with two isoforms of LC3A, GABARAP and GABARAPL1–2 (11).”
Background
Cited by
Rogov, V., Dötsch, V., Johansen, T., & Kirkin, V. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.014 · Cited by 992
Self-citationUbiquitin-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
Nguyen, T. N., Padman, B. S., Usher, J., Oorschot, V., Ramm, G., & Lazarou, M. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201607039 · Cited by 668
Mechanisms of Autophagy Initiation
Hurley, J. H., & Young, L. N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044820 · Cited by 656
Autophagy genes in biology and disease
Yamamoto, H., Zhang, S., & Mizushima, N. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-022-00562-w · Cited by 623
Metadata
- Authors
- Alemu, E. A., Lamark, T., Torgersen, K. M., Birgisdottir, A. B., Larsen, K. B., Jain, A., Olsvik, H., Øvervatn, A., Kirkin, V., & Johansen, T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-11
- Volume
- 287
- Issue
- 47
- Pages
- 39275-39290
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2001160077
- Cited by
- 288
- References
- 11
- FWCI
- 14.43
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Alemu, E. A., Lamark, T., Torgersen, K. M., Birgisdottir, A. B., Larsen, K. B., Jain, A., Olsvik, H., Øvervatn, A., Kirkin, V., & Johansen, T. (2012). ATG8 Family Proteins Act as Scaffolds for Assembly of the ULK Complex. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m112.378109
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