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Brian Scott Schaffhausen

Jaharis 606
150 Harrison Ave.
Boston, MA 02111
brian.schaffhausen@tufts.edu

office: 617-636-6876/6868
lab: 617-636-6854

Brian Schaffhausen, Ph.D.

Professor, Tufts Department of Biochemistry

Chairman, Tufts Department of Biochemistry

 

Links:

Research

Lab Members

Recent Publications

  

Research Summary:

We are interested in regulation of mammalian cell growth and cellular signal transduction. The lab is particularly interested in protein phosphorylation Most of our work starts from issues raised by polyomavirus, a small DNA tumor virus. Polyomaviruses subvert host cell mechanisms for its replication and transcription. Study of polyomaviruses has identified major mechanisms of cell regulation such as tyrosine phosphorylation, PI3 kinase and p53. The ability of the mouse virus to transform is based on its early proteins: large T (LT), middle T (MT) and small T (ST) antigens and their actions in the cell.

Research:
 

For more details, please see the publications below.

Lab Members


Recent Publications

  1. Love, Tara M; de Jesus, Rowena; Kean, Jennier A; Sheng, Qing; Leger, Andrew; Schaffhausen, Brian S. Activation of CREB/ATF Sites by Polyomavirus Large T Antigen. Journal of Virology 79:7, 4180-4190 (2005)
  2. Whalen, Kerry A; de Jesus, Rowena; Kean, Jennifer A; Schaffhausen, Brian S. Genetic Analysis of the Polyomavirus DnaJ Domain. Journal of Virology 79:15, 9982-9990 (2005)
  3. Lu, A., Zhang, H., Zhang, X., Wang, H., Hu, Q., Shen, L., Schaffhausen, B., Hou, W., Li, L. 2004. Attenuation of SARS coronavirus by a short hairpin RNA expression plasmid targeting RNA-dependent RNA polymerase. Virology 324,84.
  4. Mittag, T., Schaffhausen, B. & Gunther, U. 2004. Tracing kinetic intermediates during ligand binding. J Am Chem Soc. 126,9017.
  5. Hong, Y., Mikami, A,, Schaffhausen, B., Jun, T., & Roberts T. 2003. A new class of mutations reveals a novel function for the original phosphatidylinositol 3-kinase binding site. Proc Natl Acad Sci U S A. 100, 9434.
  6. Gunther, U., Weyrauch, B., Zhang, X., & Schaffhausen B. 2003. Nuclear magnetic resonance structure of the P395S mutant of the N-SH2 domain of the p85 subunit of PI3 kinase: an SH2 domain with altered specificity. Biochemistry 42, 11120.
  7. Mittag, T., Schaffhausen, B., Gunther, U. 2003. Direct observation of protein-ligand interaction kinetics. Biochemistry 42, 11128.
  8. Günther, U. & Schaffhausen, B. 2002. NMRKIN: Simulating Line Shapes from Two-Dimensional Spectra of Proteins, J. Biomolecular NMR 22, 201..
  9. Tian, X. Rusanescu G., Hou. W., Schaffhausen, B. & Feig, L. 2002. PDK1 Mediates Ral-GEF Activation by a Kinase-Independent Mechanism. EMBO J. 21, 1327.
  10. Gunther U, Mittag T, Schaffhausen B. 2002 Probing Src homology 2 domain ligand interactions by differential line broadening.Biochemistry. 41, 11658.
  11. Sheng,Q., Love,T. & Schaffhausen, B., 2000, J domain independent regulation of the Rb family by polyoma large T antigen. J. Virol. 74, 5280.
  12. Weber,T Schaffhausen,B., Liu , Y & Günther, U.,2000. NMR structure of the N-SH2 of the p85 subunit of PI3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosinebinding site. Biochemistry 39, 15860.
  13. Yen, A., Cherington, V., Schaffhausen, B., Marks, K., and Varvayanis, S., 1999. Transformation-defective polyoma MT mutants defective in PLCgamma, PI-3, or src kinase activation enhance ERK2 activation and promote retinoic acid-induced, cell differentiation like wild-type middle T. Exp. Cell Res.248,538.
  14. Culleré, X., Rose, P., Thathamangalam, U., Chatterjee, A., Mullane, K., Pallas, D., Benjamin, T.,Roberts, T. & Schaffhausen, B. 1998. Serine 257 phosphorylation regulates association of polyoma middle T antigen with 14-3-3 proteins. J. Virol. 72, 558.
  15. Chou, M., Hou, W., Johnson J., Graham L., Lee, M., Chen, C., Newton ,A., Schaffhausen, B. and Toker A. 1998. Regulation of protein kinase C zeta by PI 3-kinase and PDK-1. Curr Biol. 8,1069.
  16. Mullane, K., Ratnofsky, M., Culleré, X. & Schaffhausen, B. 1998. Signaling from middle T and small T defines different roles for protein phosphatase 2A. Mol. Cell. Biol. 18, 7556

 


             

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