Signal Transduction

Can we understand RB?

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Science  08 Mar 2019:
Vol. 363, Issue 6431, pp. 1053-1054
DOI: 10.1126/science.363.6431.1053-d

The tumor suppressor retinoblastoma (RB) protein is essential for normal development and suppression of aberrant cell proliferation. Its mode of action remains elusive though, in part because hundreds of proteins have been reported to interact with RB. Phosphorylation is known to alter RB structure in profound but specific ways. Sanidas et al. explored the consequences of cyclin-dependent kinase activity on 14 phosphorylation sites across RB. For example, monophosphorylation of RB at Ser811 triggers chromatin remodeling, alters the spectrum of genes repressed by RB, and promotes mitochondrial function. Monophosphorylated RBs interact with many different proteins in distinct ways to regulate multiple targets. This is just the start of understanding how the RB phosphorylation code affects cell function.

Mol. Cell. 10.1016/j.molcel.2019.01.004 (2019).

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