|Dept:||Biochemistry/Biophysics & Molc Biol-AGLS|
|Office:||3264 Molecular Bio|
The Raf family of serine-threonine kinases has been conserved in evolution with members identified from the plant and animal kingdoms. Raf proteins act to trigger phosphorylation cascades in response to their activation via receptor tyrosine kinase (RTK) and Ras signals in animal cells. The molecular mechanism of Raf signaling has been addressed in many studies, but little known about how Raf activity is converted to biological function in the organism. Such understanding is important, because in humans unregulated Raf kinase activity leads to cellular transformation and colon cancer.
In Drosophila, D-raf is a key component of numerous developmental pathways that depend on the activity of RTKs and Ras to ultimately control gene expression patterns in the nucleus. In the absence of D-raf protein activity transmission of RTK signals does not occur and instead abnormal development is observed. We are currently using a molecular genetics approach to understand the underlying mechanisms that control D-raf’s activity in normal development and to identify novel gene products that act with D-raf in these signal transduction pathways.
- Research interests
- Biological function of Raf
- B.S., Biology, SUNY Stony Brook, 1976
Ph.D., Biology, Princeton University, 1985
Postdoctoral Fellow, Harvard Medical School, 1986-1991
- Lab Research
- Studying how Raf activity is converted to biological function in the organism.