Deubiquitinating activity of CYLD is impaired by SUMOylation in neuroblastoma cells.

Tamae Kobayashi, Katarzyna Masoumi, Ramin Massoumi

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

28 Citeringar (SciVal)
469 Nedladdningar (Pure)

Sammanfattning

CYLD is a deubiquitinating (DUB) enzyme that has a pivotal role in modulating nuclear factor kappa B (NF-κB) signaling pathways by removing the lysine 63- and linear-linked ubiquitin chain from substrates such as tumor necrosis factor receptor-associated factor 2 (TRAF2) and TRAF6. Loss of CYLD activity is associated with tumorigenicity, and levels of CYLD are lost or downregulated in different types of human tumors. In the present study, we found that high CYLD expression was associated with better overall survival and relapse-free neuroblastoma patient outcome, as well as inversely correlated with the stage of neuroblastoma. Retinoic acid-mediated differentiation of neuroblastoma restored CYLD expression and promoted SUMOylation of CYLD. This posttranslational modification inhibited deubiquitinase activity of CYLD against TRAF2 and TRAF6 and facilitated NF-κB signaling. Overexpression of non-SUMOylatable mutant CYLD in neuroblastoma cells reduced retinoic acid-induced NF-κB activation and differentiation of cells, but instead promoted cell death.Oncogene advance online publication, 9 June 2014; doi:10.1038/onc.2014.159.
Originalspråkengelska
Sidor (från-till)2251-2260
TidskriftOncogene
Volym34
Nummer17
DOI
StatusPublished - 2015

Ämnesklassifikation (UKÄ)

  • Cancer och onkologi

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