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09.04.2025Surface Plasmon Resonance and orthogonal technologies reveal a new mechanism of Src regulation through lipids.
PhD. Marta Taulés Marín, head of the Molecular Interaction Analysis Laboratory at CCiTUB, has collaborated with a multidisciplinary team of researchers from the University of Barcelona (Departments of Inorganic and Organic Chemistry, Materials Science, and Chemistry and Physics), the Institute for Bioengineering of Catalonia (IBEC) and the Centre National de la Recherche Scientifique and the Université de Montpellier.
The article, published in Life Science Alliance, reveals the importance of lipid-mediated Src self-association as an additional regulatory mechanism for the oncogenic potential of the Src protein. The study shows, for the first time, the formation of condensates of this protein when it binds to lipids and that a cluster of lysines in its SH4 region is essential for its self-association.
Src, the first discovered oncogene, is a tyrosine kinase that regulates the growth, survival, and migration of cancer cells. The study suggests that changes in lipid composition can affect Src self-association and its oncogenic capacity in human cells.
For these studies, the Surface Plasmon Resonance (SPR) equipment from CCiTUB was used. This is a Biacore T200 (Cytiva) device with a Xantec chip derivatized with phytosphingosine to capture the liposomes to be studied and keep the reference channel free of lipophilic substances. The data were doubly referenced and analysed with the BiaEval software (Cytiva).
SPR allows distinguishing monomeric forms, which can be removed with washes, from self-associated forms that bind persistently. Since dimers represent a small fraction of Src, detection was performed with antibodies. The ability to detect different species, without specific labelling, and separable by their different dissociation kinetics is a distinguishing feature that makes SPR the ideal technique for these studies.