The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins
Open accessAbstract
The mitophagy receptor Nix interacts with LC3/GABARAP proteins, targeting mitochondria into autophagosomes for degradation. Here we present evidence for phosphorylation-driven regulation of the Nix:LC3B interaction. Isothermal titration calorimetry and NMR indicate a ~100 fold enhanced affinity of the serine 34/35-phosphorylated Nix LC3-interacting region (LIR) to LC3B and formation of a very rigid complex compared to the non-phosphorylated sequence. Moreover, the crystal structure of LC3B in complex with the Nix LIR peptide containing glutamic acids as phosphomimetic residues and NMR experiments revealed that LIR phosphorylation stabilizes the Nix:LC3B complex via formation of two additional hydrogen bonds between phosphorylated serines of Nix LIR and Arg11, Lys49 and Lys51 in LC3B. Substitution of Lys51 to Ala in LC3B abrogates binding of a phosphomimetic Nix mutant. Functionally, serine 34/35 phosphorylation enhances autophagosome recruitment to mitochondria in HeLa cells. Together, this study provides cellular, biochemical and biophysical evidence that phosphorylation of the LIR domain of Nix enhances mitophagy receptor engagement.
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Nix is a selective autophagy receptor for mitochondrial clearance
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Essential role for Nix in autophagic maturation of erythroid cells
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Self-citationStructural Basis for Sorting Mechanism of p62 in Selective Autophagy
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Response to myocardial ischemia/reperfusion injury involves Bnip3 and autophagy
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Self-citationUbiquitin-independent function of optineurin in autophagic clearance of protein aggregates
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Mitochondrial Pruning by Nix and BNip3: An Essential Function for Cardiac-Expressed Death Factors
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Mitophagy, Mitochondrial Homeostasis, and Cell Fate
Ma, K., Chen, G., Li, W., Kepp, O., Zhu, Y., & Chen, Q. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00467 · Cited by 594
Quality control of the mitochondrion
Ng, M. Y. W., Wai, T., & Simonsen, A. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.009 · Cited by 445
Yao, R.-Q., Ren, C., Xia, Z.-F., & Yao, Y.-M. (2021) · Autophagy · doi:10.1080/15548627.2020.1725377 · Cited by 441
Mechanisms of Selective Autophagy
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Metadata
- Authors
- Rogov, V. V., Suzuki, H., Marinković, M., Lang, V., Kato, R., Kawasaki, M., Buljubašić, M., Šprung, M., Rogova, N., Wakatsuki, S., Hamacher-Brady, A., Dötsch, V., Dikic, I., Brady, N. R., & Novak, I.
- Venue
- Scientific Reports
- Published
- 2017-04-25
- Volume
- 7
- Issue
- 1
- Pages
- 1131-1131
- ISSN
- 2045-2322 (ISSN-L)
- OpenAlex
- W2605825818
- Cited by
- 297
- References
- 9
- FWCI
- 13.91
- Type
- journal article
- Language
- en
- Open access
- gold
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- Rogov, V. V., Suzuki, H., Marinković, M., Lang, V., Kato, R., Kawasaki, M., Buljubašić, M., Šprung, M., Rogova, N., Wakatsuki, S., Hamacher-Brady, A., Dötsch, V., Dikic, I., Brady, N. R., & Novak, I. (2017). Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins. Scientific Reports. https://doi.org/10.1038/s41598-017-01258-6
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