The Proteomics Laboratory utilises advanced bioanalytical techniques to better understand how protein molecules and complexes are regulated in health and disease.
Proteins mediate key biological functions and many diseases are caused by the deregulation of normal protein homeostasis. In the Proteomics Laboratory we use cutting edge technology to analyse the chemical and biochemical properties of proteins from different standpoints including their expression, localisation, binding partners, post-translational modifications and enzymatic activity. In order to discover new regulatory mechanisms at the protein biochemistry level, we aim to use innovative analytical approaches for unbiased global or targeted protein characterisation, and quantification using labelled or label-free approaches.
The laboratory is equipped with two LTQ Orbitrap LC-MS mass spectrometers (LTQ XL and LTQ Velos) and a Q-Exactive quadrupole orbitrap instrument. We have expertise in many different aspects of proteomics including:
- Quantitative analysis of protein phosphorylation.
- Characterisation of dynamic protein-protein interactions.
- Subcellular proteomics.
- Analysis of enzymatic activities by mass spectrometry.
- Proteomics and peptidomics of biological fluids to understand the mechanisms of physiological processes and for the discovery of disease biomarkers.
We use in-house modified software to analyse quantitative proteomic data, which was designed and written in order to quantify proteins and their modifications without the need for isotopic labelling. Working closely with the CSC researchers to understand the biological question they are interested in exploring, we use these proteomic technologies to decipher how the dynamic proteome contributes to the regulation of cell biology and disease.
The Proteomics Laboratory uses standardised sample preparation procedures and protocols to maximise the amount of information that can be gleaned from a sample, whether submitted for proteomic or phosphoproteomic analyses.
Rotival M, Ko JH, Srivastava PK, Kerloc’h A, Montoya A, Mauro C, Faull P, Cutillas PR, Petretto E, Behmoaras J Integrating phosphoproteome and transcriptome reveals new determinants of macrophage multinucleation, Mol Cell Proteomics (2014 Dec 22) pii: mcp.M114.043836. [Epub ahead of print]
Silva N, Ferrandiz N, Barroso C, Tognetti S, Lightfoot J, Telecan O, Encheva V, Faull P, Hanni S, Furger A, Snijders AP, Speck C, Martinez-Perez, E The Fidelity of Synaptonemal Complex Assembly Is Regulated by a Signaling Mechanism that Controls Early Meiotic Progression Dev Cell (2014 Nov 24) 31(4):503-11. doi: 10.1016/j.devcel.2014.10.001. Epub 2014 Nov 6.