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@ARTICLE{Shi:300185,
      author       = {H. Shi and Y. Yang and J. Gao and S. Kumar and H. Xie and
                      Z. Chen and J. Lyu and H. Sihto and V. Koljonen and S.
                      Vega-Rubin-de-Celis and V. Vukojevic and F. Farnebo and V.
                      Björnhagen and A. Höög and C. C. Juhlin and L. Lee and M.
                      Wickström and J. C. Becker$^*$ and J. I. Johnsen and C.
                      Larsson and W.-O. Lui},
      title        = {{K}it-mediated autophagy suppression driven by a viral
                      oncoprotein emerges as a crucial survival mechanism in
                      {M}erkel cell carcinoma.},
      journal      = {Autophagy},
      volume       = {21},
      number       = {7},
      issn         = {1554-8627},
      address      = {Abingdon, Oxon},
      publisher    = {Taylor $\&$ Francis},
      reportid     = {DKFZ-2025-00662},
      pages        = {1523-1543},
      year         = {2025},
      note         = {ISSN 1554-8635 / 2025 Jul;21(7):1523-1543},
      abstract     = {The KIT/c-KIT proto-oncogene is frequently over-expressed
                      in Merkel cell carcinoma (MCC), an aggressive skin cancer
                      commonly caused by Merkel cell polyomavirus (MCPyV). Here,
                      we demonstrated that truncated MCPyV-encoded large T-antigen
                      (LT) suppressed macroautophagy/autophagy by stabilizing and
                      sequestering KIT in the paranuclear compartment via binding
                      VPS39. KIT engaged with phosphorylated BECN1, thereby
                      enhancing its association with BCL2 while diminishing its
                      interaction with the PIK3C3 complex. This process ultimately
                      resulted in the suppression of autophagy. Depletion of KIT
                      triggered both autophagy and apoptosis, and decreased LT
                      expression. Conversely, blocking autophagy in KIT-depleted
                      cells restored LT levels and rescued apoptosis.
                      Additionally, stimulating autophagy efficiently increased
                      cell death and inhibited tumor growth of MCC xenografts in
                      mice. These insights into the interplay between MCPyV LT and
                      autophagy regulation reveal important mechanisms by which
                      viral oncoproteins are essential for MCC cell viability.
                      Thus, autophagy-inducing agents represent a therapeutic
                      strategy in advanced MCPyV-associated MCC.Abbreviation:
                      3-MA, 3-methyladenine; AL, autolysosome; AP, autophagosome;
                      Baf-A1, bafilomycin A1; BARA, β-α repeated autophagy
                      specific domain; BH3, BCL2 homology 3 domain; CCD,
                      coiled-coil domain; CHX, cycloheximide; Co-IP,
                      co-immunoprecipitation; CQ, chloroquine; CTR, control; DAPI,
                      4',6-diamidino-2-phenylindole; EBSS, Earle's balanced salt
                      solution; ECD, evolutionarily conserved domain; EEE,
                      three-tyrosine phosphomimetic mutations Y229E Y233E Y352E;
                      ER, endoplasmic reticulum; FFF, three-tyrosine
                      non-phosphomimetic mutations; FFPE, formalin-fixed
                      paraffin-embedded; FL, full-length; GIST, gastrointestinal
                      stromal tumor; IB, immunoblotting; IHC,
                      immunohistochemistry; KIT-HEK293, KIT stably expressing
                      HEK293 cells; KRT20/CK20, keratin 20; LT, large T-antigen;
                      LT339, MCPyV truncated LT antigen; LTco, codon-optimized
                      MCPyV LT antigen; MCC, Merkel cell carcinoma; MCPyV-,
                      MCPyV-negative; MCPyV, Merkel cell polyomavirus; MCPyV+,
                      MCPyV-positive; PARP1, poly(ADP-ribose) polymerase 1; PCI,
                      pan-caspase inhibitor; PI, propidium iodide; PtdIns3K, class
                      III phosphatidylinositol 3-kinase; PtdIns3P,
                      phosphatidylinositol-3-phosphate; RB1, RB transcriptional
                      corepressor 1; RTKs, receptor tyrosine kinases; KITLG/SCF,
                      KIT ligand; sT, small T-antigen; sTco, codon-optimized MCPyV
                      sT antigen; T-B, Tat-BECN1; T-S, Tat-scrambled; TEM,
                      transmission electron microscopy.},
      keywords     = {Autophagy (Other) / BECN1 (Other) / KIT (Other) / Merkel
                      cell carcinoma (Other) / Merkel cell polyomavirus (Other) /
                      large T antigen (Other)},
      cin          = {ED01},
      ddc          = {570},
      cid          = {I:(DE-He78)ED01-20160331},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40108758},
      doi          = {10.1080/15548627.2025.2477385},
      url          = {https://inrepo02.dkfz.de/record/300185},
}