Fabien Heuze

Bioengineer, Candidate for a PhD
Laboratory of Bioinformatics and Modelling
GIGA research center
Liege University
F.Heuze@ulg.ac.be


  1. Brief presentation
  2. Hi everyone! A little bit about myself first...In September 2009, I graduated from Gembloux Agro-Bio Tech as Bioengineer in Biotechnology and crop protection, "summa cum laude". Right now, I am a first year FNRS (Belgian National Fund for Scientific Research) PhD student, at Liege University.

    The main focus of my thesis will be on "Intrinsically Disordered Proteins" (IDPs).

    IDPs are proteins which can adopt a wide range of secondary and/or tertiary structures, when alone in solution (Uversky et al., 2009). For this reason, they can adapt their structure according to the partner that they bind. Different programs, based on experimental data or on sequence information, predicted that up to 30% of eukaryotic proteomes is intrinsically disordered (Dunker et al., 2000, 2008; Ward et al., 2004; Tompa, 2002). Moreover, IDPs present a particular interest since proteins that are involved in at least 10 interactions (i.e., hubs) in different eukaryotic proteomes have been identified as being significantly more disordered than proteins involved in only one interaction (i.e. end proteins) (Haynes et al., 2006; Barrios-Rodiles et al., 2005). In addition, these ID-hub proteins revealed to be involved in many key cell-signaling and regulation pathways as well as in several critical diseases such as cancers, neurodegenerative diseases, diabetes, cardiovascular diseases (Iakoutcheva et al., 2002; Mayo and Donner, 2002; Van Heyningen and Yeyati, 2004). In accordance with these observations, enrichment of different types of post-translational modifications has been found in disordered regions (Iakoucheva et al., 2004), e.g. phosphorylation which "has emerged as a ubiquitous regulatory switch in cell signaling networks" (Collins, 2009). Finally, IDPs seem to have rather different binding mechanisms than fully structured proteins. All this suggests that a refinement of our current knowledge about this intriguing class of "chameleon" proteins could be highly valuable, at fundamental and applied level as well.

  3. Previous work/publications
  4. Resume

  5. CV

  6. Contact