Fuyuhiko Tamanoi

Fuyuhiko Tamanoi

310-825-7754

Laboratory Address:
Molecular Science Building 2711, 2715
Los Angeles, CA 90095

Office Address:
405 Hilgard Avenue
Los Angeles, CA 90095

Work Address:
Molecular Science Building 2610A
BOX 951489
Los Angeles, CA 90095

Fax Number:
310-206-5231

Work Phone Number:
310-206-7318

http://www.cnsi.ucla.edu/arr/personnel-papers?personnel_id=45741
http://www.mimg.ucla.edu/faculty/tamanoi/

Affiliations

Director, JCCC Signal Transduction and Therapeutics Program Area
Professor, Microbiology, Immunology & Molecular Genetics
Member, CTSI, California NanoSystems Institute, Cell & Developmental Biology GPB Home Area, Molecular Pharmacology GPB Home Area

Research Interests

The Ras-superfamily G-proteins play critical roles in cell growth and differentiation. Our research focuses on two members, Ras and Rheb. Ras is mutated in a wide range of human cancer including pancreatic, lung and colon cancers. This GTPase plays a central role in the growth factor signal transduction that is initiated by the activation of a receptor tyrosine kinase and results in the activation of multiple downstream pathways such as the Raf/Mek/Erk. Rheb is a novel and unique member of the Ras superfamily G-proteins. We have identified Rheb homologues in a number of organisms including fruit fly and yeasts, and defined unique features of this family of G-protein. Genetic studies using fission yeast as well as Drosophila showed that Rheb plays critical roles in cell growth, regulation of cell cycle and nutrient uptake. Rheb is a component of the TSC/TOR/S6K signaling pathway and is a direct activator of TOR. Rheb is downregulated by Tsc1/Tsc2 complex that acts as a GTPase activating protein (GAP) for Rheb. Mutations in the Tsc1 or Tsc2 gene leads to a genetic disorder called tuberous sclerosis that is associated with the appearance of benign tumors at multiple sites in the body. Our current effort is aimed at defining proteins involved in the Rheb signaling pathway. Both Ras and Rheb proteins are farnesylated, and the farnesylation is critical for their function. In particular, membrane association and transforming activity of Ras is dependent on its farnesylation. This led to the development of small molecule inhibitors of protein farnesyltransferase. These inhibitors, called FTIs, have recently been evaluated as anti-cancer drugs. FTIs block anchorage-independent growth of a wide variety of human cancer cells and animal studies have shown that FTIs inhibit the growth of tumors or even regress tumor growth. Our study focuses on the mechanism how FTI affects human cancer cells.

Biography

Fuyu Tamanoi is a biochemist who has served on the UCLA School of Medicine and UCLA College faculty since he joined the Department of Microbiology, Immunology & Molecular Genetics in 1993. He became a full professor in 1997. Since 1996, he has been a Director of Signal Transduction Program Area at Jonsson Comprehensive Cancer Center. Dr. Tamanoi earned his B.S. and M.S. in Biochemistry at the University of Tokyo. He received PhD in Molecular Biology at Nagoya University in 1977. He was a postdoctoral fellow at Harvard Medical School, where he worked on bacteriophage DNA replication. From 1980 to 1985, he was a senior staff investigator at Cold Spring Harbor Laboratory, where he worked on adenovirus DNA replication. From 1985 to 1993, he was an Assistant Professor and then Associate Professor at the University of Chicago, where he initiated studies on lipid modification of the Ras family proteins. His laboratory research centers on signal transduction and signal transduction inhibitors. He is currently exploring ways to deliver signal transduction inhibitors using nanoparticles.

Publications

A selected list of publications: