Caratterizzazione dell'affinità di legame della filamina C e dei suoi partner FATZ-1 e miotilina nel disco Z del muscolo

Skeletal and cardiac muscles, essential to animal fitness, are composed of thin and thick filaments arranged in sarcomere, the basic contractile unit. Z-discs are found at the boundaries of adjacent sarcomeres and play a crucial role in transmitting forces and initiating various signaling pathways. They are composed of over 40 proteins, including Filamin C (FLNc), a key Z-disc component, functioning as both a structural scaffold by cross-linking actin filaments and a mechano-sensing signaling hub by interacting with numerous binding partners. FATZ-1 and myotilin are such partners, with their interaction being vital for Z-disc functionality. Previous studies have provided insights into their interaction, yet many questions remain. Our project aims to assess the interaction between FLNc and its ligands using different biochemical methods sucj as fluorescence anisotropy and isothermal titration calorimetry to measure binding affinities, stoichiometry, and thermodynamics. Specifically, we investigated FLNc interactions with d91FATZ-1 and myotilin250-444. The results show that our system is functioning and binding can be observed to determine a dissociation constant (Kd).