Seth M Rubin
|Title||Associate Professor, |
Director PBSE Graduate Program
|Division||Physical & Biological Sciences|
|Department||PBSci-Chemistry & Biochemistry Department|
|Phone||831-459-1921 (Office), |
|Web Site||Rubin Research Group|
|Office||Physical Sciences Bldg 262 (Office), |
Physical Sciences Bldg 298 (Lab)
|Campus Mail Stop||Chemistry|
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.
Biography, Education and Training
B.A. Columbia University
Ph.D. University of California, Berkeley
Postdoctoral Fellow, Memorial Sloan Kettering Cancer Center
Liban T.L., Thwaites M.J., Dick F.A., Rubin S.M. Structural conservation and E2F binding specificity within the retinoblastoma pocket protein family. J Mol Biol. 2016 Oct 9;428(20):3960-3971.
Marceau A.H., Felthousen J.G., Goestch P.D., Iness A.N., Lee H.W., Tripathi S.M., Strome S., Litovchick L., Rubin S.M. Structural basis for LIN54 recognition of CHR elements in cell cycle regulated promoters. Nat Commun. 20 June 2016 Accepted. Published online 28 July 2016.
Pye C.R., Bray W.M., Brown E.R., Burke J.R., Lokey R.S., Rubin S.M. A strategy for direct chemical activation of the retinoblastoma protein. ACS Chem Biol. 2016 May 20;11(5):1192-7.
Guiley K.Z, Liban T.J., Felthousen J.G., Ramanan, P., Tripathi S.M., Litovchick L., Rubin S.M. Structural mechanisms of DREAM complex assembly and regulation. Genes Dev. 2015 May 1;29(9):961-774.
Burke J.R., Liban T.J., Restrepo T., Lee H.W., Rubin S.M. Multiple mechanisms for E2F binding inhibition by phosphorylation of the retinoblastoma protein C-terminal domain. J Mol Biol. 2014 Jan 9;426(1):245-55.
McGrath D.A., Balog E.R.M., Kõivomägi M., Lucena R., Mai M.V., Hirschi A., Kellogg D.R., Loog M., Rubin S.M. Cks confers specificity to phosphorylation-dependent Cdk signaling pathways. Nat Struct Mol Biol., 2013 Dec;20(12):1407-14.
Dick F.A., Rubin S.M. Molecular mechanisms underlying RB protein function. Nat Rev Mol Cell Biol. 2013 May;14(5):297-306.
Rubin S.M. Deciphering the retinoblastoma protein phosphorylation code. Trends Biochem Sci. 2013 Jan;38(1):12-9.
Burke J.R., Hura G.L., Rubin S.M. Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. Genes Dev. 2012 Jun 1;26(11):1156-66.
Balog E.R.M., Saetern OC, Finch W., Hoeft C.O., Thai V., Harvey S.L., Kellogg D.R., Rubin S.M. The structure of a monomeric mutant Cks protein reveals multiple functions for a conserved hinge-region proline. J Mol Biol. 2011 Aug. 19; 411(3):520-8.
Hirschi A., Cecchini M., Steinhardt R.C., Schamber M.R., Dick F.A., Rubin S.M. An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein. Nat Struct Mol Biol. 2010 Sep;17(9):1051-7.
Burke J.R., Deshong A.J., Pelton J.G., Rubin S.M. Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding. J Biol Chem. 2010 May 21;285(21):16286-93.