|
|
||||||||||||
|
| |||||||||||||
|
JACK
E. DIXON
TEL: 858-822-3529 FAX: 858-534-6573 email: jedixon@ucsd.edu website: http://cmm.ucsd.edu/lab_pages/dixon Ph.D., University of California, Santa Barbara Key Words: Protein Tyrosine Phosphatases (PTPases) Cells are highly responsive to signals from their environment. These signals include growth factors, neuronal firing, or even the presence of a bacteria or pathogen that has invaded the body. The sensing and processing of these signals are carried out by molecular circuits within the cell which detect, amplify and integrate these signals into a specific response. One of the most widely utilized cellular responses to environmental signals is to change the phosphorylation strategy of specific proteins. The level of protein phosphorylation is controlled by two families of enzymes known as protein kinases and phosphatases. My laboratory is interested in deciphering the role of the phosphatases in various cellular paradigms, as phosphatases play key roles in the ontogeny of cancer as well as the processes of axonal pathfinding and bacterial pathogenesis. Selected Publications: Das S, Dixon JE, Cho W. (2003). Membrane-binding and activation mechanism of PTEN. Proc Natl Acad Sci U S A. 100:7491-6. Shao F, Dixon JE. (2003). YopT is a cysteine protease cleaving Rho family GTPases. Adv Exp Med Biol. 529:79-84. Kim SA, Vacratsis PO, Firestein R, Cleary ML, Dixon JE. (2003). Regulation of myotubularin-related (MTMR)2 phosphatidylinositol phosphatase by MTMR5, a catalytically inactive phosphatase. Proc Natl Acad Sci U S A. 100:4492-7. McDonald C, Vacratsis PO, Bliska JB, Dixon JE. (2003). The yersinia virulence factor YopM forms a novel protein complex with two cellular kinases. J Biol Chem. 278:18514-23. Shao F, Vacratsis PO, Bao Z, Bowers KE, Fierke CA, Dixon JE. (2003). Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases. Proc Natl Acad Sci U S A. 100: 904-9. Wishart MJ, Dixon JE. (2002). PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease. Trends Cell Biol. 12: 579-85. |
|
|||||||||||
|
|
|||||||||||||
|
|
|
|
|
||||||||||
|
Main address: Department of Pharmacology, University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093-0636 pharmhr@ucsd.edu Terms and Conditions of Use Copyright ©2003 Regents of the University of California. All rights reserved. |