The Thévenin Lab

Membrane Protein Biophysics: Transduction and Modulation of Receptor Signaling

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Membrane Biophysics & Drug Delivery

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We are interested in understanding how transmembrane helix interactions in cell membranes modulate the activity of integral membrane proteins. Integral membrane proteins are involved in almost every aspect of cell biology and physiology. Consequently, proper functioning of these proteins is vital to health, and defects are associated with many known diseases. However, the structural features and mechanisms that govern signal transduction across cell membrane and oligomerization are not well known or described. Our research seeks to gain structural and mechanistic insights into the role of these interactions in normal physiological functions and diseases. We also seek to develop novel biomedical technologies targeting transmembrane interactions and the activity of cytoplasmic signaling proteins in cancer cells. The interdisciplinary nature of this work involves a wide range of biophysical, biochemical and biological approaches, and is collaborative. We work in close contact with the Engelman and the DiMaio Labs at Yale University.



Delivery of therapeutic peptides into cancer cells


Peptides that interfere with protein interactions have great potential as anticancer agents. However, their low stability and poor tumor penetration limit their use. To circumvent these difficulties and specifically target and deliver peptides to cancer cells, we use the pHLIP peptide. Read More...

Activation mechanism of the thrombopoietin receptor


The thrombopoietin receptor (TpoR) regulates the production of platelets. Its single TM domain is thought to be involved in the process of receptor dimerization and activation, but its exact role is poorly defined. We seek to understand the signaling activation of TpoR and to define the mechanism of small-molecule agonists.

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Role of the trasmembrane helix in RPTPs activity


Receptor Protein-Tyrosine Phosphatase (RPTPs) are essential to many cell processes, but unlike their counterparts (i.e. the receptor protein kinases), the mechanisms controlling their activity remain to be understood. Particularly, the role of the TM domain in this process remains mainly unexplored.

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There are openings for undergraduate and graduate students. Please, email for more information about availability and specific research projects.