Interdisciplinary Life Science - PULSe Great research is a matter of choice

Angeline Lyon

Angeline Lyon Profile Picture

Assistant Professor of Chemistry and Biological Sciences
Ph.D. - 2009 - University of Texas at Austin


Contact Info:

lyon5@purdue.edu


Training Group(s):
Biomolecular Structure and Biophysics
Membrane Biology


Current Research Interests:

 Cardiovascular disease is a growing problem worldwide and the leading cause of death in the United States. Phospholipase C (PLC) enzymes, in particular PLCß and PLCe, are essential for normal cardiovascular function and generate the second messengers diacylglycerol (DAG) and inositol-1,4,5-triphosphate (IP3), which in turn lead to increases in intracellular calcium and activation of protein kinase C. Abnormally high levels of DAG and IP3 can cause cardiac arrhythmias, hypertrophy, and heart failure. PLCß and PLCe respond to various extracellular signals that serve to regulate the production of these second messengers. PLCß is activated downstream of G protein-coupled receptors, such as the angiotensin receptor, via direct interactions with the heterotrimeric G protein subunits Gaq and Gß?. PLCe integrates and amplifies signals from both G protein-coupled receptors and receptor tyrosine kinases via direct interactions with small molecular weight G proteins such as Ras and Rho.

The goals of our lab are to understand the molecular mechanisms regulating PLCß and PLCe under basal and activating conditions. These studies incorporate biochemical and cell-based functional assays along with an innovative combination of X-ray crystallography and electron cryo-microscopy. Taken together, these studies will provide much needed insight into two key enzymes that contribute to cardiovascular function and disease, and will ultimately aid in the identification and development of novel therapeutics that modulate signaling by these enzymes.



Selected Publications:

Lyon, A.M., Begley, J.A., Manett, T., and Tesmer, J.J.G. Regulation of Phospholipase Cß by Progressive Destabilization. Structure. 22, 1844-1854 (2014). PMID: 25435326.

Lyon, A.M., Taylor, V. G., and Tesmer, J. J. G. Strike a Pose: Gaq Complexes at the Membrane. Trends in Pharmacological Sciences 35, 23-30 (2014). PMID: 24287282.

Lyon, A.M. and Tesmer J. J. G. Structural insights into phospholipase C-ß function. Mol. Pharm. 84, 488-500 (2013). PMID: 23880553.

Lyon, A.M., Dutta, S., Skiniotis, G., and Tesmer, J.J.G. Characterization of phospholipase C-ß3 complexes by X-ray crystallography and single particle cryo-electron microscopy. Transactions of the American Crystallographic Association (2013).

Lyon, A.M., Dutta, S., Boguth, C.A., Skiniotis, G., and Tesmer, J.J.G. Structure of Full-Length Phospholipase C ß3 in Complex with Gaq Reveals Functional Interfaces of its C-terminal Coiled-Coil Domain. Nat. Struct. Mol. Biol. 20, 355-362 (2013). PMCID: PMC3594540.

Lyon, A.M., Tesmer, V.M., Dhamsania, V. D., Thal, D.M., Gutierrez, J., Chowdhury, S., Suddala, K., Northup, J.K., and Tesmer, J.J.G. An Autoinhibitory Helix in the C-Terminal Region of Phospholipase Cß Represses Basal Activity and Mediates Gaq Activation. Nat. Struct. Mol. Biol. 18, 999-1005 (2011). PMCID: PMC3168981 (Faculty of 1000 selection).

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