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Proteolysis of MOB1 by the ubiquitin ligase praja2 attenuates Hippo signalling and supports glioblastoma growth.

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Lignitto L,Arcella A,Sepe M,Rinaldi L,Delle Donne R,Gallo A,Stefan E,Bachmann VA,Oliva MA,Tiziana Storlazzi C,L'Abbate A,Brunetti A,Gargiulo S,Gramanzini M,Insabato L,Garbi C,Gottesman ME,Feliciello A

doi

10.1038/ncomms2791

subject

Has Abstract

pub_date

2013-01-01 00:00:00

pages

1822

issn

2041-1723

pii

ncomms2791

journal_volume

4

pub_type

杂志文章

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