个人简介

B.A. Columbia University Ph.D. University of California, Berkeley Postdoctoral Fellow, Memorial Sloan Kettering Cancer Center

研究领域

Biochemistry and biophysical chemistry; molecular mechanisms of cell cycle regulation, nuclear magnetic resonance, x-ray crystallography

Our broad research interests are in understanding the biochemical mechanisms that control the cell cycle. Cell growth and division are carefully coordinated by a shifting network of biomolecular interactions. Protein interactions regulate enzymatic activities responsible for key cell cycle events such as DNA replication, chromosome segregation, and cytokinesis. These events have strict spatial and temporal requirements for proper cell cycle function, and deregulation of protein interaction networks is commonly associated with aberrant cell proliferation and cancer. Understanding mechanisms of cell cycle control requires a detailed molecular picture of protein-protein interactions and how these interactions regulate enzymatic function and cellular architecture. Our laboratory seeks to elucidate the biochemical determinants of protein interaction affinity and specificity and how these factors are affected by regulatory modifications to protein composition and structure. We apply a variety of structural and biochemical techniques to learn in molecular detail how structural changes and chemical modifications affect biological function.

近期论文

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Deciphering the retinoblastoma protein phosphorylation code. Trends Biochem Sci. 2013 Jan;38(1):12-9. Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. Genes Dev. 2012 Jun 1;26(11):1156-66. The Structure of a Monomeric Mutant Cks Protein Reveals Multiple Functions for a Conserved Hinge-Region Proline. Balog ER, Saetern OC, Finch W, Hoeft CO, Thai V, Harvey SL, Kellogg DR, Rubin SM. J Mol Biol. 2011 Jun 17. An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein. Hirschi A, Cecchini M, Steinhardt RC, Schamber MR, Dick FA, Rubin SM. Nat Struct Mol Biol. 2010 Sep;17(9):1051-7. Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding. Burke JR, Deshong AJ, Pelton JG, Rubin SM. J Biol Chem. 2010 May 21;285(21):16286-93. Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. Rubin SM, Gall AL, Zheng N, Pavletich NP. Cell. 2005 Dec 16;123(6):1093-106.