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Sandra S Rossie


  • Professor of Biochemistry
BCHM Room 315

 General Information

Area of Expertise: Signal transduction and protein Ser/Thr phosphatases

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, environmental 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 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 is 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 physiological 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.

Department of Biochemistry, 175 South University Street, West Lafayette, IN 47907-2063 USA, (765) 494-1600

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