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@ARTICLE{Rogov:120656,
      author       = {V. V. Rogov and H. Suzuki and M. Marinković and V.
                      Lang$^*$ and R. Kato and M. Kawasaki and M. Buljubašić and
                      M. Šprung and N. Rogova and S. Wakatsuki and A.
                      Hamacher-Brady$^*$ and V. Dötsch and I. Dikic and N.
                      Brady$^*$ and I. Novak},
      title        = {{P}hosphorylation of the mitochondrial autophagy receptor
                      {N}ix enhances its interaction with {LC}3 proteins.},
      journal      = {Scientific reports},
      volume       = {7},
      number       = {1},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {DKFZ-2017-01083},
      pages        = {1131},
      year         = {2017},
      abstract     = {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.},
      cin          = {B190},
      ddc          = {000},
      cid          = {I:(DE-He78)B190-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28442745},
      pmc          = {pmc:PMC5430633},
      doi          = {10.1038/s41598-017-01258-6},
      url          = {https://inrepo02.dkfz.de/record/120656},
}