βKlotho filters ligand-independent FGFR1/4-PLCΓ signaling to prevent aberrant constitutive Ca 2+ entry

influx. Together, our findings identify βKlotho as a specialized signaling filter that safeguards FGFR signaling fidelity by uncoupling deleterious PLCγ-TRPC6 signaling while maintaining canonical MAPK output. These results reveal a previously unrecognized ligand-independent role of βKlotho in reconfiguring the FGFR signaling architecture.