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cc-by (c) Iruela Martin, Guillermo et al., 2022
Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/184607

A FRET-based biosensor for the N-terminal regulatory element

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In signaling proteins, intrinsically disordered regions often represent regulatory elements, which are sensitive to environmental effects, ligand binding, and post‐translational modifications. The conformational space sampled by disordered regions can be affected by environmental stimuli and these changes trigger, vis a vis effector domain, downstream processes. The disordered nature of these regulatory elements enables signal integration and graded responses but prevents the ap‐ plication of classical approaches for drug screening based on the existence of a fixed three‐dimen‐ sional structure. We have designed a genetically encodable biosensor for the N‐terminal regulatory element of the c‐Src kinase, the first discovered protooncogene and lead representative of the Src family of kinases. The biosensor is formed by two fluorescent proteins forming a FRET pair fused at the two extremes of a construct including the SH4, unique and SH3 domains of Src. An internal control is provided by an engineered proteolytic site allowing the generation of an identical mixture of the disconnected fluorophores. We show FRET variations induced by ligand binding. The bio‐ sensor has been used for a high‐throughput screening of a library of 1669 compounds with seven hits confirmed by NMR.

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IRUELA MARTÍN, Guillermo, FERNÁNDEZ, Alejandro, SAGAR, Amin, CARVAJAL, Francisco javier, BERNADÓ PERETÓ, Pau, PONS VALLÈS, Miquel. A FRET-based biosensor for the N-terminal regulatory element. _Biosensors-Basel_. 2022. Vol. 12, núm. 2, pàgs. 96. [consulta: 20 de gener de 2026]. ISSN: 2079-6374. [Disponible a: https://hdl.handle.net/2445/184607]

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