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@ARTICLE{Postlmayr:310338,
      author       = {A. Postlmayr and A. Sanchez Bergman and J. Torrejon Diaz
                      and B. Ciraulo and S. Yan and N. Hofmann$^*$ and S. Carbajal
                      and R. Dobler and C. Machaalani and M. T. Schönholzer and
                      L. Priego Gonzalez and A. J. De Micheli and E.
                      Berenjeno-Correa and L. Baroncini and M. A. Grotzer and U.
                      Tabori and C. Hawkins and O. Ayrault and M. Zuckermann$^*$
                      and M. Baumgartner and A. S. Guerreiro Stücklin},
      title        = {{F}unctionally distinct {ALK} and {ROS}1 fusions detected
                      in infant-type hemispheric gliomas converge on {STAT}3 and
                      {SHP}2 activation.},
      journal      = {Cell reports},
      volume       = {45},
      number       = {3},
      issn         = {2211-1247},
      address      = {Maryland Heights, MO},
      publisher    = {Cell Press},
      reportid     = {DKFZ-2026-00539},
      pages        = {117046},
      year         = {2026},
      note         = {#NCTZFB26#},
      abstract     = {ALK and ROS1 fusions are key drivers of infant-type
                      hemispheric gliomas (IHG). With diverse gene partners, the
                      impact of ALK and ROS1 oncoprotein heterogeneity on glioma
                      biology remains unknown. We developed an integrative
                      phospho-proteomic and transcriptomic approach to discover
                      biological functions regulated by five IHG-associated
                      fusions: CCDC88A::ALK, PPP1CB::ALK, GOPC::ROS1, CLIP1::ROS1,
                      and KIF21A::ROS1. Here, we report fusion-specific oncogenic
                      functions conferred by the 5' gene partner, including
                      increased cell motility driven by microtubule-interacting
                      fusions CCDC88A::ALK and CLIP1::ROS1. All studied fusions
                      converge on STAT3 activation. Using affinity purification
                      mass spectrometry, we identified SHP2 in direct interaction
                      with all three ROS1 oncoproteins but with none of the ALK
                      oncoproteins, which in turn interact with SHC1/SHC3. ROS1
                      fusions phosphorylate SHP2 to a greater extent than ALK
                      fusions, and analyses of downstream pathways suggest
                      MAPK-independent, non-canonical SHP2-driven functions. Our
                      findings reveal both common and fusion-specific
                      dependencies, offering opportunities to optimize therapeutic
                      strategies for pediatric gliomas.},
      keywords     = {ALK (Other) / CP: cancer (Other) / ROS1 (Other) / STAT3
                      (Other) / brain tumors (Other) / cell motility (Other) /
                      cell signaling (Other) / gene fusions (Other) / infant-type
                      hemispheric gliomas (Other) / pediatric gliomas (Other) /
                      receptor tyrosine kinases (Other)},
      cin          = {B062 / HD02},
      ddc          = {610},
      cid          = {I:(DE-He78)B062-20160331 / I:(DE-He78)HD02-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41790556},
      doi          = {10.1016/j.celrep.2026.117046},
      url          = {https://inrepo02.dkfz.de/record/310338},
}