% 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{Infante:132650,
      author       = {P. Infante and R. Faedda and F. Bernardi and F. Bufalieri
                      and L. Lospinoso Severini and R. Alfonsi and D. Mazzà and
                      M. Siler and S. Coni and A. Po and M. Petroni and E.
                      Ferretti and M. Mori and E. De Smaele and G. Canettieri and
                      C. Capalbo and M. Maroder and I. Screpanti and M. Kool$^*$
                      and S. Pfister$^*$ and D. Guardavaccaro and A. Gulino and L.
                      Di Marcotullio},
      title        = {{I}tch/β-arrestin2-dependent non-proteolytic
                      ubiquitylation of {S}u{F}u controls {H}edgehog signalling
                      and medulloblastoma tumorigenesis.},
      journal      = {Nature Communications},
      volume       = {9},
      number       = {1},
      issn         = {2041-1723},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {DKFZ-2018-00310},
      pages        = {976},
      year         = {2018},
      abstract     = {Suppressor of Fused (SuFu), a tumour suppressor mutated in
                      medulloblastoma, is a central player of Hh signalling, a
                      pathway crucial for development and deregulated in cancer.
                      Although the control of Gli transcription factors by SuFu is
                      critical in Hh signalling, our understanding of the
                      mechanism regulating this key event remains limited. Here,
                      we show that the Itch/β-arrestin2 complex binds SuFu and
                      induces its Lys63-linked polyubiquitylation without
                      affecting its stability. This process increases the
                      association of SuFu with Gli3, promoting the conversion of
                      Gli3 into a repressor, which keeps Hh signalling off.
                      Activation of Hh signalling antagonises the Itch-dependent
                      polyubiquitylation of SuFu. Notably, different SuFu
                      mutations occurring in medulloblastoma patients are
                      insensitive to Itch activity, thus leading to deregulated Hh
                      signalling and enhancing medulloblastoma cell growth. Our
                      findings uncover mechanisms controlling the tumour
                      suppressive functions of SuFu and reveal that their
                      alterations are implicated in medulloblastoma
                      tumorigenesis.},
      cin          = {B062 / L101},
      ddc          = {500},
      cid          = {I:(DE-He78)B062-20160331 / I:(DE-He78)L101-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29515120},
      pmc          = {pmc:PMC5841288},
      doi          = {10.1038/s41467-018-03339-0},
      url          = {https://inrepo02.dkfz.de/record/132650},
}