Robert Stahelin

rstaheli View All Faculty

Biography

Professor Stahelin received his B.S. in biochemistry from the University of Illinois-Chicago in 1998. He earned his Ph.D. in chemistry from the University of Illinois-Chicago in 2003 for studying the structural basis of lipid-protein interactions in health and disease. During postdoctoral work at the University of Illinois-Chicago he investigated the mechanisms with which bioactive lipid signals recruit peripheral proteins in cell signaling and membrane trafficking. He joined the Notre Dame and Indiana University School of Medicine-South Bend faculty in July of 2006 and was promoted to Associate Professor in 2012.

Back to Top

Research Interests

Interdisciplinary research focused on biological membranes has revealed them as signaling and trafficking platforms for processes fundamental to life. Biomembranes harbor receptors, ion channels, lipid domains, lipid signals, and scaffolding complexes, which function to maintain cellular growth, metabolism, and homeostasis. Moreover, abnormalities in lipid metabolism attributed to genetic changes among other causes are often associated with diseases such as cancer, arthritis and diabetes. Thus, there is a need to comprehensively understand molecular events occurring within and on membranes as a means of grasping disease etiology and identifying viable targets for drug development. A rapidly expanding field in the last decade has centered on understanding membrane recruitment of peripheral proteins. This class of proteins reversibly interacts with specific lipids in a spatial and temporal fashion in crucial biological processes. Typically, recruitment of peripheral proteins to the different cellular sites is mediated by one or more modular lipid-binding domains through specific lipid recognition. Structural, computational, and experimental studies of these lipid-binding domains have demonstrated how they specifically recognize their cognate lipids and achieve subcellular localization. However, the mechanisms by which these modular domains and their host proteins are recruited to and interact with various cell membranes often vary drastically due to differences in lipid affinity, specificity, penetration as well as protein-protein and intramolecular interactions. As there is still a paucity of predictive data for peripheral protein function, these enzymes are often rigorously studied to characterize their lipid-dependent properties. Our research is targeted at identifying peripheral protein drug targets, designing predictive functions for this class of proteins, and understanding their biological mechanisms of activation as a means of creating better therapies. The below points highlight the different avenues of research in the Stahelin lab:

1. Molecular Basis of Viral Assembly.
We are investigating how viruses such as the Ebola virus assembles at the plasma membrane of human cells to form the bud site for generation of a new viral particle.  Funded by NIAID.
 
2. Discovery of New Lipid-Binding Domains. Integration of computational biology, bioinformatics, structural biology, biochemistry, biophysics, and cell biology to discover new lipid-binding domains in the human genome.
 
3. Lipid-Mediated Regulation of Proinflammatory Enzymes. We are elucidating the role of phosphoinositides and sphingolipids in the regulation of proinflammatory enzymes. Funded by the AHA.

 

Back to Top

Recent Papers

Ward, K.E., Bhardwaj, N.n Vora, M., Chalfant, C.E., Lu, H. and Stahelin, R.V. "The molecular basis of ceramide-1-phosphate recognition by C2 domains" (2013) J. Lipid Res., 54, 636-648. Featured on the cover of the March 2013 issue.

Link

Adu-Gyamfi, E., Soni, S.P., Xue, Y., Digman, M.A., Gratton, E., and Stahelin, R.V. "The Ebola virus matrix protein penetrates into the plasma membrane: a key step in viral protein 40 (VP40) oligomerization and egress" (2013) J. Biol. Chem., 288, 5779-5789.

Link

Adu-Gyamfi, E., Digman, M.A., Gratton, E., and Stahelin, R.V. "Single-particle tracking demonstrates that actin coordinates the movement of the Ebola virus matrix protein" (2012) Biophys. J., 103, L41-L43.

Link

Ward, K.E., Ropa, J.P., Adu-Gyamfi, E., and Stahelin, R.V. "C2 domain membrane penetration by group IVA cytosolic phospholipase A2 induces membrane curvature changes" (2012) J. Lipid Res., 53, 2656-2666.

Link

Adu-Gyamfi, E., Digman, M.A., Gratton, E., and Stahelin, R.V. "Investigation of Ebola VP40 assembly and oligomerization in live cells using number and brightness analysis" (2012) Biophys. J., 102, 2517-2525.

Link

Bhattacharjee, S., Stahelin, R.V., Speicher K.D., Speicher, D.W., and Haldar, K. "Endoplasmic reticulum PI(3)P lipid binding targets malaria proteins to the host cell" (2012) Cell, 148, 201-212.

Link

Back to Top

Back to Top


Contact Information

Primary Research Areas

Research Specialties

Lab Personnel

Courses