OUR WORK

Protein phosphorylation is a critical post translational modification consisting of the covalent attachment of an inorganic phosphate to serine, threonine or tyrosine residues. Protein kinases are responsible for the addition of these phosphate groups and substrate conformational changes induced by phosphate groups can lead to alteration of protein activity, subcellular location or biomolecular interactions, which in turn regulate biological processes such as proliferation, differentiation or cell death. Under physiological conditions, kinase-driven signalling pathways are able to transduce an adequate response to a particular intra or extracellular signal. However, alterations of these signaling pathways can produce an erroneous response to a signal, a lack of response or response in the absence of the signal. These dysregulated signaling pathways contribute to the appearance of pathological conditions such as cancer, diabetes or neurodegeneration. In this sense, we are focused on brain cancer malignancies and brain metastasis to investigate the properties of signalling pathways that are dysregulated in these cancer models. Several kinase inhibitors are approved for the treatment of cancer and many more are being developed as potential drugs for cancer treatment.

Phosphoproteomics provides relevant information for the design and implementation of kinase inhibitor-based therapies and how to use it in translational research. This technique is ideal for the prediction and monitoring of resistance to drugs that target cell signalling networks. Phosphoproteomics has been successfully used to rationalize responses to kinase inhibitors, to identify drug targets, and for the development of new therapies against several malignancies, including cancer and neurodegenerative diseases. Large efforts have been recently put in the identification of biomarkers that can predict the clinical efficacy of kinase inhibitors and other drugs. Thus, significant advances have been achieved using phosphoproteomics studies.