Retinoblastoma

Scientists at Washington University report research in retinoblastoma

Published in Proteomics Weekly, February 4th, 2008

"The activity of Rb (retinoblastoma protein) is regulated by phosphorylation and acetylation events. Active Rb is hypo-phosphorylated and acetylated on multiple residues," scientists writing in the Biochemical Journal report.

"Inactivation of Rb involves concerted hyper-phosphorylation by cyclin-CDK (cyclin-dependent kinase) complexes combined with deacetylation of appropriate lysine residues within Rb. In the present study, using it' vivo co-immunoprecipitation experiments, we identified mammalian SIRT1 (sirtuin 1) as a binding partner for Rb and its family members p107 and p130. Formation of Rb-SIRT1 complexes required the pocket domain of Rb. p300 catalysed...

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Source: Proteomics Weekly (2008-02-04)

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