Sandra S. Rossie

Sandra S.  Rossie Profile Picture

Associate Professor of Biochemistry
Ph.D. - 1984 - University of Chicago

Contact Info:

Training Group(s):
Cancer Biology
Integrative Neuroscience

PULSe Contributor - not currently hosting students for laboratory rotations or recruiting students in the laboratory

Current Research Interests:

Reversible phosphorylation is an important and common mechanism for regulating a wide variety of processes ranging from cellular excitation to gene expression. 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. Little is known about PP5's biological function, however this enzyme is implicated in controlling cell growth and in hormone signal transduction pathways. We are using biochemical and molecular approaches to define the role and regulation of PP5 in brain and other tissues. Projects are focused on the structural basis for controlling PP5 activity, identification of physiologic substrates and regulators for PP5, and examination of the regional and subcellular distribution of PP5. These studies will advance our understanding of PP5's function and the role that Ser/Thr protein phosphatases play in signal transduction pathways in brain and elsewhere.

Selected Publications:

Rossie, S. Regulation of Voltage-Sensitive Ion Channels by Phosphorylation. In: Advances in Second Messenger and Phosphoprotein Research vol. 33 (Armstrong, D. and Rossie, S. eds.) (1999) Academic Press, San Diego, CA.

Sinclair, C., Borchers, C., Parker, C., Tomer, K., Charbonneau, H. and Rossie, S. (1999) The tetratricopeptide repeat domain and a C-terminal region control the activity of ser/thr protein phosphatase 5. J. Biol. Chem. 274: 23666-23672.

Skinner, J., Sinclair, C., Romeo, C., Armstrong, D., Charbonneau, H. and Rossie, S. (1997) Purification of a fatty acid-stimulated protein Ser/Thr phosphatase from bovine brain and its identification as a homolog of protein phophatase 5. J. Biol. Chem. 272: 22464-22471.

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