Laurence LEVY
  • E-mail :[email]
  • Phone : +33 1 49 28 46 11
  • Location : Paris, France
Last update 2013-05-21 17:12:00.985

Laurence LEVY PhD in molecular genetics

Course and current status

Research positions:

• Since 2009: INSERM CR2 position at CDR Saint-Antoine, Paris, INSERM U938. Study of Arkadia/RNF111 E3 ubiquitin-ligase in signaling and tumorigenesis.

• 2008-2009: Postdoc Fellow at CDR Saint-Antoine, Paris, INSERM U938 (Lab Head: Azeddine Atfi). Study of E3 ubiquitin-ligase in TGF-β/Smad signaling and tumorigenesis.

• 2003-2008: Postdoc Fellow at CRUK Lincoln Inn's Field, London (Lab Head: Caroline Hill). Study of TGF-β/Smad signaling in tumorigenesis.

• 1998-2003: PhD Fellow at Pasteur Institute, Paris, INSERM U163 (Lab Head: Pierre Tiollais/ supervisor: Marie-Annick Buendia). Study of Wnt/β-caténine pathway in tumorigenesis


2003 : PhD in genetics, (UPMC, Paris 6)

1998 : - Master2/DEA  "Génétique Cellulaire et Moléculaire", (UPMC, Paris 6)

           - Magister of Biologie-Biochimie (ENS-Ulm, Paris)

Scientific summary

During my Postdoc, I have identified the E3 ubiquitin ligase  Arkadia/RNF111 as an important modulator of the TGF-b signaling pathway that enables activation of the pathway by inducing degradation of the transcriptional repressor SnoN/Ski (Levy et al , Mol Cell Biol, 2007). Interestingly, I have discovered a deletion mutation of Arkadia/RNF111 in cancer that generates a truncated protein devoid of RING domain and have demonstrated that this mutation abolishes SnoN degradation and TGF-b signaling, suggesting that Arkadia mutations might trigger tumor progression (Briones-Orta/Levy et al, cancer research, 2013). Recently I have shown that Arkadia also contains three successive SUMO interacting motifs (SIMs) that mediate non-covalent interaction with SUMO, an ubiquitin-like peptide that can also be attached to proteins. I have demonstrated that Arkadia binds specifically to poly-sumoylated proteins and provide evidence that Arkadia can triggers ubiquitination of sumoylated proteins (Erker et al, Mol Cell Biol, 2013). I am currently studying this new Sumo-Target Ubiqutin Ligase function (STUBL) of Arkadia by investigating its potential role in different crutial cellular process where ubiquitination and sumoylation are involved.

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