Protein Interaction Networks
We are interested in understanding cell and organism properties from the analysis of genome wide protein interaction networks.
Our long term goal is the development of an in silico cell that could be used experimentally to test our understanding of
physiological and evolutionary processes.
We aim at developing technology in order to contribute to the community effort to assemble a complete and biologically reliable
protein interaction network. To this end we use peptide libraries displayed on bacteriophages and peptides chemically synthesized
on high density arrays to probe the recognition specificity of families of peptide recognition domains.
We are interested in characterizing the interaction network mediated by the binding of protein domains (SH3, SH2, PDZ, WW, 14-3-3 etc) and their peptide targets.
Our experimental projects are complemented and supported by a strong investment in a bioinformatics approach.
Our group has developed the protein interaction database MINT containing, in a structured and easily searchable format,
the protein interaction information published in the scientific literature. MINT is integrated in an international collaboration
with four major protein interaction databases (Intact, Bind, MIPS, DIP) to establish a common standard for the capture of protein interaction information
to facilitate data sharing.
A biological test
Finally the structure of the networks obtained through the high throughput experiments and their informatic analysis are put
to a test in a biological settings by applying the approach to the analysis of the mechanisms underlying the control of the
EGF receptor endocytosis in animal cells. This part of the project is carried out in collaboration with the group of L. Castagnoli.
This project aims at characterizing in great detail and in a quantitative manner the interaction network between the proteins regulating receptor endocytosis