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Protein phosphorylation is central to cell cycle signal integration. Phosphorylation of regulatory proteins on multiple sites generates manifold responses and intricate signaling properties. A common model for the function of multisite Cyclin-dependent kinase (Cdk) phosphorylation is that sites are redundant in function but together tune signaling sensitivity. In contrast, my laboratory has been studying two cell cycle contexts in which phosphorylation on specific sites induces distinct structural and biochemical effects. First, I will describe our recent efforts in characterizing the Cdk subunit Cks as a specificity factor for Cdk activity. We find that Cks binds specific phosphorylated sequences in Cdk substrates in order to facilitate processive phosphorylation and associate Cdk with its regulators. Second, I will describe our structural characterization of Retinoblastoma protein (Rb) inactivation. Rb is an important tumor suppressor protein and negative regulator of S phase. We find that discrete phosphorylation events induce diverse Rb structures that inhibit different Rb-protein interactions. These observations suggest that multisite phosphorylation serves as a code for inducing distinct functional outputs.

Department:  Biology

Contact: Maria Magana-Lopez | 650-723-2413 | mmagana@stanford.edu

Presenter(s):

• Seth Rubin University of California, Santa Cruz

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