Lewis Cantley

Department of Cell Biology

Harvard Medical School

Division of Signal Transduction

BIH Harvard Institutes of Medicine

4 Blackfan Circle, 10th floor

Boston, MA 02115

tel: (617) 667-0947; fax (617) 667-0957

email: cantley@helix.mgh.harvard.edu

Cantley lab home page

The long term research objective of this laboratory is to understand the biochemical basis for mammalian cell growth regulation and transformation. In particular, we are trying to understand the structural basis for specificity and regulation of protein kinases and phosphatidylinositol kinases that have been implicated in mammalian cell growth control. This research involves the cloning and expression of sufficient quantities of these proteins for in vitro studies. In addition, mutant forms of the proteins are added back to cells to determine the role of the proteins in cellular responses. Recently, we have developed a new 'oriented peptide library' technique that allows us to quickly determine the optimal peptide sequence for binding to specific catalytic or regulatory sites of protein kinases. This approach provides rapid results that are providing new insights into the structural basis for protein/protein interactions.

Selected Publications:

Songyang, Z., Lu, K. P., Kuan, Y., Tsai, L.-H., Filhol, O., Cochet, C., Soderling, T. R., Bartleson, C., Graves, D. J., Hoekstra, M. F., Blenis, J., Hunter, T. and Cantley, L. C. (1996) A Structural Basis for Substrate Specificities of Protein Ser/Thr-Kinases: Primary Sequence Preferences of Casein Kinase I and II, NIMA, Phosphorylase Kinase, Cam Kinase II, CDK5 and Erk1. Mol. Cell. Biol. 16, 6486-6493.

Rameh, L. E., Chen, C.-S., and Cantley, L. C. (1995) Phosphatidylinositol-3,4,5-P3 Interacts with SH2 Domains and Modulates Phosphoinositide 3-kinase Association with Tyrosine-Phosphorylated Proteins. Cell 83, 821-830.

Songyang, Z., Fanning, A. S., Fu, C., Xu, J., Marfatia, S. M., Chishti, A. H., Crompton, A., Chan, A. C., Anderson, J. M. and Cantley, L. C. (1997) Recognition of Unique Carboxyl-terminal Motifs by Distinct PDZ Domains. Science 275, 73-77.