% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Pantoom:163508,
      author       = {Pantoom, Supansa and Pomorski, Adam and Huth, Katharina and
                      Hund, Christina and Petters, Janine and Krężel, Artur and
                      Hermann, Andreas and Lukas, Jan},
      title        = {{D}irect {I}nteraction of {ATP}7{B} and {LC}3{B} {P}roteins
                      {S}uggests a {C}ooperative {R}ole of {C}opper
                      {T}ransportation and {A}utophagy.},
      journal      = {Cells},
      volume       = {10},
      number       = {11},
      issn         = {2073-4409},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {DZNE-2022-00268},
      pages        = {3118},
      year         = {2021},
      note         = {(CC BY)},
      abstract     = {Macroautophagy/autophagy plays an important role in
                      cellular copper clearance. The means by which the copper
                      metabolism and autophagy pathways interact mechanistically
                      is vastly unexplored. Dysfunctional ATP7B, a
                      copper-transporting ATPase, is involved in the development
                      of monogenic Wilson disease, a disorder characterized by
                      disturbed copper transport. Using in silico prediction, we
                      found that ATP7B contains a number of potential binding
                      sites for LC3, a central protein in the autophagy pathway,
                      the so-called LC3 interaction regions (LIRs). The conserved
                      LIR3, located at the C-terminal end of ATP7B, was found to
                      directly interact with LC3B in vitro. Replacing the two
                      conserved hydrophobic residues W1452 and L1455 of LIR3
                      significantly reduced interaction. Furthermore, autophagy
                      was induced in normal human hepatocellular carcinoma cells
                      (HepG2) leading to enhanced colocalization of ATP7B and LC3B
                      on the autophagosome membranes. By contrast, HepG2 cells
                      deficient of ATP7B (HepG2 ATP7B-/-) showed autophagy
                      deficiency at elevated copper condition. This phenotype was
                      complemented by heterologous ATP7B expression. These
                      findings suggest a cooperative role of ATP7B and LC3B in
                      autophagy-mediated copper clearance.},
      keywords     = {Amino Acid Sequence / Biological Transport: drug effects /
                      Copper: metabolism / Copper: pharmacology /
                      Copper-Transporting ATPases: chemistry / Copper-Transporting
                      ATPases: metabolism / Hep G2 Cells / Humans /
                      Microtubule-Associated Proteins: metabolism / Protein
                      Binding: drug effects / Protein Transport: drug effects /
                      ATPase copper transporting beta (Other) / HepG2 (Other) /
                      LC3 interaction region (Other) / Wilson disease (Other) /
                      autophagosome-lysosome fusion (Other) / MAP1LC3B protein,
                      human (NLM Chemicals) / Microtubule-Associated Proteins (NLM
                      Chemicals) / Copper (NLM Chemicals) / ATP7B protein, human
                      (NLM Chemicals) / Copper-Transporting ATPases (NLM
                      Chemicals)},
      cin          = {AG Teipel},
      ddc          = {570},
      cid          = {I:(DE-2719)1510100},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34831341},
      pmc          = {pmc:PMC8625360},
      doi          = {10.3390/cells10113118},
      url          = {https://pub.dzne.de/record/163508},
}