% 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{Wakabayashi:138900,
      author       = {Wakabayashi, Satoru and Sawamura, Naoya and Voelzmann,
                      André and Brömer, Meike and Asahi, Toru and Hoch, Michael},
      title        = {{O}hgata, the {S}ingle {D}rosophila {O}rtholog of {H}uman
                      {C}ereblon, {R}egulates {I}nsulin {S}ignaling-dependent
                      {O}rganismic {G}rowth.},
      journal      = {The journal of biological chemistry},
      volume       = {291},
      number       = {48},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.60645},
      reportid     = {DZNE-2020-05222},
      pages        = {25120-25132},
      year         = {2016},
      abstract     = {Cereblon (CRBN) is a substrate receptor of the E3 ubiquitin
                      ligase complex that is highly conserved in animals and
                      plants. CRBN proteins have been implicated in various
                      biological processes such as development, metabolism,
                      learning, and memory formation, and their impairment has
                      been linked to autosomal recessive non-syndromic
                      intellectual disability and cancer. Furthermore, human CRBN
                      was identified as the primary target of thalidomide
                      teratogenicity. Data on functional analysis of CRBN family
                      members in vivo, however, are still scarce. Here we identify
                      Ohgata (OHGT), the Drosophila ortholog of CRBN, as a
                      regulator of insulin signaling-mediated growth. Using ohgt
                      mutants that we generated by targeted mutagenesis, we show
                      that its loss results in increased body weight and organ
                      size without changes of the body proportions. We demonstrate
                      that ohgt knockdown in the fat body, an organ analogous to
                      mammalian liver and adipose tissue, phenocopies the growth
                      phenotypes. We further show that overgrowth is due to an
                      elevation of insulin signaling in ohgt mutants and to the
                      down-regulation of inhibitory cofactors of circulating
                      Drosophila insulin-like peptides (DILPs), named acid-labile
                      subunit and imaginal morphogenesis protein-late 2. The two
                      inhibitory proteins were previously shown to be components
                      of a heterotrimeric complex with growth-promoting DILP2 and
                      DILP5. Our study reveals OHGT as a novel regulator of
                      insulin-dependent organismic growth in Drosophila.},
      keywords     = {Adaptor Proteins, Signal Transducing / Animals / Cell Line
                      / Drosophila Proteins: genetics / Drosophila Proteins:
                      metabolism / Drosophila melanogaster / Gene Knockdown
                      Techniques / Humans / Insulins: genetics / Insulins:
                      metabolism / Peptide Hydrolases: genetics / Peptide
                      Hydrolases: metabolism / Signal Transduction: physiology /
                      Ubiquitin-Protein Ligases / CRBN protein, human (NLM
                      Chemicals) / Drosophila Proteins (NLM Chemicals) / Ilp5
                      protein, Drosophila (NLM Chemicals) / Insulins (NLM
                      Chemicals) / Peptide Hydrolases (NLM Chemicals)},
      cin          = {AG Brömer 1},
      ddc          = {540},
      cid          = {I:(DE-2719)5000021},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27702999},
      pmc          = {pmc:PMC5122779},
      doi          = {10.1074/jbc.M116.757823},
      url          = {https://pub.dzne.de/record/138900},
}