Sandra Rossie
Professor of Biochemistry
 |
Area |
The structure, regulation, and function of protein Ser/Thr phosphatase 5 |
| Office
| HANS 221A |
| Phone
| (765) 494-3112 |
| Email
| rossie@purdue.edu |
| Degree |
Ph.D. University of Chicago, 1984 |
Reversible phosphorylation is an important and common mechanism for regulating a wide variety of processes in response to incoming signals such as hormones and neurotransmitters, enviromental changes or cell damage. In contrast to our knowledge of protein kinases and their roles in these processes, we know far less about protein phosphatases and their regulation. Protein phosphatase 5 (PP5) is a recently described member of the largest Ser/Thr protein phosphatase family, with a unique N-terminal domain that inhibits PP5 activity and binds other proteins PP5 has been implicated in signal transduction pathways controlling cell growth, differentiation and apoptosis, or programmed cell death. Little is known, however, about the physiological substrates for PP5 or how its activity may be regulated.
We use biochemical and molecular approaches to define the role and regulation of PP5 in brain and other tissues. Projects include defining the structural basis for controlling PP5 activity and potential regulators of PP5 activity. We are also using a proteomics approach to identify physiological substrates for PP5. We focus on the role of PP5 in neurons and in cancer cells, since the pathways in which PP5 may function are key players in neurodegenerative diseases and in tumor cell proliferation.
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