http://www.cnr.it/ontology/cnr/individuo/prodotto/ID298676
Proteolysis of MOB1 by the ubiquitin ligase praja2 attenuates Hippo signalling and supports glioblastoma growth (Articolo in rivista)
- Type
- Label
- Proteolysis of MOB1 by the ubiquitin ligase praja2 attenuates Hippo signalling and supports glioblastoma growth (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1038/ncomms2791 (literal)
- Alternative label
Lignitto, Luca; Arcella, Antonietta; Sepe, Maria; Rinaldi, Laura; Delle Donne, Rossella; Gallo, Adriana; Stefan, Eduard; Bachmann, Verena A.; Oliva, Maria A.; Storlazzi, Clelia Tiziana; L'Abbate, Alberto; Brunetti, Arturo; Gargiulo, Sara; Gramanzini, Matteo; Insabato, Luigi; Garbi, Corrado; Gottesman, Max E.; Feliciello, Antonio (2013)
Proteolysis of MOB1 by the ubiquitin ligase praja2 attenuates Hippo signalling and supports glioblastoma growth
in Nature communications
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Lignitto, Luca; Arcella, Antonietta; Sepe, Maria; Rinaldi, Laura; Delle Donne, Rossella; Gallo, Adriana; Stefan, Eduard; Bachmann, Verena A.; Oliva, Maria A.; Storlazzi, Clelia Tiziana; L'Abbate, Alberto; Brunetti, Arturo; Gargiulo, Sara; Gramanzini, Matteo; Insabato, Luigi; Garbi, Corrado; Gottesman, Max E.; Feliciello, Antonio (literal)
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- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- University of Naples Federico II; IEOS CNR; IRCCS Neuromed Localita Camerelle; Inst Biochem; CMBI; University of Bari; University of Naples Federico II; University of Naples Federico II; Columbia University; CNR IBB (literal)
- Titolo
- Proteolysis of MOB1 by the ubiquitin ligase praja2 attenuates Hippo signalling and supports glioblastoma growth (literal)
- Abstract
- 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. (literal)
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