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Christian Griesinger, November 24th... R. Dos santos Morais, 30/11/2017, 4... Takahiro Muraoka, 16/11/2017, 11am,... Vladimir Torbeev, 9/11/2017, 2pm, E... M. D. Smith & T.Constantieux, 3/11/... James Nowick, 15 september 2017, 11... Emmanuelle Thinon, 28 June 2017, 11... Caroline Tokarski, 15 June 2017, 4p... Christian Salesse, 8 June 2017, 4pm... Patrice Rey, 01 June 2017, 2h30 pm,... Christina Sizun, 18 May 2017, 4 pm,... Marisela Velez, 5 May 2017, 11am, I... Iqbal Choudhary, 27 April 2017, 4 p... Vincent Aucagne, 21 April 2017, 11 ... Sophie Zinn-Justin, 14 April 2017, ... Cécile Feuillie, 16 February 2017,... Félix M. Goñi, 8 december 2016, 4... Félix M. Goñi, 17 november 2016, ... Carl Creutz, 20 october 2016, 4 pm,... Diego Romero, 30 september 2016, 11... A. Ciaccafava, 8 september 2016, 14... A. Ramamoorthy, 16 June 2016, 16h,... Alexandre de Brevern, 2 june 2016, ... Isabelle Landrieu, 26 May, 16h, ENS... Frances Sepavoric, 12 May, 16h, ENS... Thomas Pradeu, 7 April 2016, 9h, EN... Françoise Argoul, 3 march 2016, 1... Corinne Loutelier-Bourhis, 16/12/20... Aristotelis XENAKIS, 3 december 201... Fabian Kiessling, 26 november 2015,... Michaël Molinari, 20 november 2015... Dipankar Das Sarma, 28 October 2015... Olivier Donard, 22 october 2015, 16... E. Morvan & A.Grelard, 17/12/2015, ... Christophe Cullin, 10 september 201... Brigitte Lindet, 18 June 2015, 16h,... Marion Decossas, 4 June 2015, 16h, ... Pascale Schellenberger, 21 Mai 2015... F. Leal-Calderon, 7 May 2015, 16h, ... Ibrahim Abdulhalim, 9 April 2015, 1... Manon Carré, 26 March 2015, 14h, ... C. Bure & JM Schmitter, 19 March 20... T. Ogata & H. Ihara, 17 March 2015,... Banafshe Larijani, 12 March 2015, 1...
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Emmanuelle Thinon, 28 June 2017, 11 am, IECB

The seminar will take place, the 28th of June 2017, at 11 am, in the IECB amphitheatre, 2 rue Robert Escarpit Pessac.

 

Chemical approaches to study protein fatty acylation

 

Emmanuelle Thinon

1 Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, 1230 York Avenue, New York, NY, 10065, USA.

2 The Crick Institute, 215 Euston Road, London, NW1 2BE, UK.

 

abstract

Protein fatty acylation (FA) is the addition of a long chain fatty acid to Glycine, Cysteine, or Lysine residues of a protein. This post-translational modification (PTM) enables direct interaction with cell membranes, and regulates protein function and localization. N-myristoylation and S-palmitoylation are the most common FAs found in all Eukaryotes, and are important in normal function and disease. However, the diversity, abundance, and regulatory mechanisms of protein FA in vivo are not fully understood. In addition, the intricate interplay of these modifications in the disease context presents a challenge for drug development.

 

FA of proteins can be studied by metabolic tagging with small, 'clickable' chemical reporters that do not disrupt normal metabolism and function. Subsequent chemoselective reactions enable the selective addition of multifunctional labels to tagged fatty acylated proteins. A fluorophore label allows visualization of the fatty acylated proteins by in-gel fluorescence, while a biotin label allows for enrichment on streptavidin beads for global whole-proteome profiling of protein FA.

 

In the first study, this labeling technology was used to validate N-myristoyltransferase (NMT), the enzyme that adds myristoyl group to proteins, as a drug target in cancer therapy. A small library of inhibitors was screened, and their on-target activity was demonstrated in cells. N-myristoylated proteins in cancer cells were identified by quantitative chemical proteomics using a combination of the best inhibitor, and the clickable chemical reporter. NMT inhibition was found to induce ER stress, cell cycle arrest, and apoptosis in cancer cells.

 

The second study involved S-palmitoylation of proteins. S-palmitoylation remains more challenging to study due to its reversibility, the presence of multiple S-palmitoylating enzymes, and the lack of selective inhibitors. The labeling technology was used, in combination with other methods, to perform S-palmitoylation whole-proteome profiling, direct site identification, and lipid structure characterization. The function of S-palmitoylation of proteins involved in vesicular transport was also studied.

 

All these studies will ultimately help in understanding the functions and regulatory mechanisms of fatty-acylated proteins in physiology and disease.

 

Short CV

 

After a master’s in Organic Chemistry in Strasbourg (ECPM) and spending 6 months under the guidance of Gilles Guichard, Emmanuelle Thinon obtained her PhD in Chemical Biology in 2014 from Imperial College London under the supervision of Ed Tate and David Mann, working on developing chemical tools to validate N-myristoyltransferase as a new target in cancer therapy. She is now a Marie Skłodowska-Curie Postdoctoral Fellow at the Rockefeller University in Howard Hang’s group and at the Crick institute in Sharon Tooze’s group, where she is developing chemical proteomics methods to identify S-lipidated proteins and studying the function of lipid modifications on proteins involved in vesicular transport.

 

Contact: Gilles Guichard, g.guichard@iecb.u-bordeaux.fr

 

 

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