Proteomics - Gif (SICaPS)
Created in 2007 under the name SICaPS (Service d’Identification et Caractérisation des Protéines par spectrométrie de masse), the Proteomics-Gif platform offers proteomics methodologies and mass spectrometry technologies to identify, characterize and quantify proteins and some of their modifications from samples of varying complexity.
The platform, which has been awarded the IBiSA label, has solid expertise in the preparation of protein samples of various types, their analysis by mass spectrometry and the analysis of the data. It advises users, optimizes and develops analytical methods in response to the needs of users and biological questions, and offers training to users, either on an ad hoc basis (Training link) or on request.
Two support teams participate in the development of proteomic strategies: the team “Protein Maturation, Protein Cellular Fate and Therapeutics” (I2BC, CNRS UMR 9198, Gif-sur-Yvette) directed by Carmela Giglione and the team “Protein Merepliement and Aggregation in Neurodegenerative Diseases” (LMN, CNRS UMR 9199, CEA, Fontenay-aux-Roses) directed by Ronald Melki .
The platform, open to academic and industrial laboratories, is part of the Ile de France Proteomic Platforms network.
The Proteomics-Gif platform is also involved in methodological optimizations and developments (sample preparation, mass spectrometry, data analysis) in order to support the projects of the research teams and to reinforce its expertise.
The main areas of optimization and development carried out on the platform meet the needs of the collaborative research projects of many users, and the projects of the two research teams that support the platform, These include the analysis of interactomes (Ronald Melki’s team “Mérepliement et agrégation des protéines dans les maladies neurodégénératives”, LMN, UMR 9199, CNRS, CEA, Fontenay-aux Roses) and N-terminomes (Carmela Giglione’s team, “Maturation des protéines, destinée cellulaire des protéines et thérapeutique”, I2BC, UMR 9198, CNRS, Gif-sur-Yvette) :
Analysis and comparison of proteomes and interactomes
By relative quantification approaches without labeling, from complex protein samples.
In-depth comparison of proteomes, subproteomes, and interactomes
From very complex and low abundance protein samples, by relative quantification approaches without labeling using the new performance of timsTOF Pro (Bruker).
Relative quantification of proteins.
Example of the analysis of the rhythmic oscillation of the ubiquitylated proteome during a circadian cycle using dedicated bioinformatic tools (Szabo A et al, Cell Report 2018, 23: 2273;)
Analysis of membrane interactomes
Example of the identification of membrane interactants (in yellow) of Tau protein fibers (Shrivastava an, EMBO J. 2019, 38:pii:e99871)
Modifications of isolated or mixed proteins
Post-translational modifications (phosphorylations, acetylations, lipids, ...)
Example of the identification of a new post-translational truncation in the C-terminus of tubulins
(Aillaud C, et al. Mol Biol Cell. 2016 Feb 15;27(4):640-53).
Example of the identification of a covalent complex suggesting a novel mechanism of regulation of strigolactone perception in plants. (De Saint Germain, Nat. Chem. Biol. 2016)
Modified N-terminal peptides of proteins:
Strategies for identification and relative quantification between samples of all protein N-terminal peptides (Bienvenut WV et al, Meth Mol Biol.2017, 1574: 17)
Structural determinants of proteins or protein complexes
Identification of covalent bridges
Examples of protein interaction surface mapping by covalent bridging approaches.
Identification of interaction surfaces between monomeric α-Synuclein and the molecular chaperone Hsc70 (Nury C; Redeker V, et al, Anal Chem. 2015, 87: 1853)
Head of Facility
ISO 9001-NFX50 900 (Qualité)