Communications Biology (Jan 2022)

SMURF2 phosphorylation at Thr249 modifies glioma stemness and tumorigenicity by regulating TGF-β receptor stability

  • Manami Hiraiwa,
  • Kazuya Fukasawa,
  • Takashi Iezaki,
  • Hemragul Sabit,
  • Tetsuhiro Horie,
  • Kazuya Tokumura,
  • Sayuki Iwahashi,
  • Misato Murata,
  • Masaki Kobayashi,
  • Akane Suzuki,
  • Gyujin Park,
  • Katsuyuki Kaneda,
  • Tomoki Todo,
  • Atsushi Hirao,
  • Mitsutoshi Nakada,
  • Eiichi Hinoi

DOI
https://doi.org/10.1038/s42003-021-02950-0
Journal volume & issue
Vol. 5, no. 1
pp. 1 – 10

Abstract

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Hiraiwa et al. show that phosphorylation of SMAD specific E3 ubiquitin protein ligase 2 (SMURF2) at Thr249 mediates ubiquitylation and degradation of the TGF-β receptor TGBR1 leading to loss of glioblastoma stem cell tumorigenic capacity. Their data elucidates a mechanism of regulation of the TGF-β signaling pathway that controls the stem cell status in glioblastoma.