Journal
NATURE COMMUNICATIONS
Volume 4, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms2791
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Funding
- Associazione Italiana per la Ricerca sul Cancro [IG 11788]
- UICC 'Yamagiwa-Yoshida Memorial International Cancer Study Grant'
- Schaefer Research Scholar Award, Columbia University NY
- Austrian Science Fund (FWF) [P22608]
- Austrian Science Fund (FWF) [P 22608] Funding Source: researchfish
- Austrian Science Fund (FWF) [P22608] Funding Source: Austrian Science Fund (FWF)
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Human glioblastoma is the most frequent and aggressive form of brain tumour in the adult population. Proteolytic turnover of tumour suppressors by the ubiquitin-proteasome system is a mechanism that tumour cells can adopt to sustain their growth and invasiveness. However, the identity of ubiquitin-proteasome targets and regulators in glioblastoma are still unknown. Here we report that the RING ligase praja2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumour-suppressor Hippo cascade. Degradation of Mob through the ubiquitin-proteasome system attenuates the Hippo cascade and sustains glioblastoma growth in vivo. Accordingly, accumulation of praja2 during the transition from low- to high-grade glioma is associated with significant downregulation of the Hippo pathway. These findings identify praja2 as a novel upstream regulator of the Hippo cascade, linking the ubiquitin proteasome system to deregulated glioblastoma growth.
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