Scientists discuss the legacy and future of GCaMP calcium indicators.
have developed GCaMP8 — optimized forms of genetically engineered calcium indicators, which respond to intracellular changes in the levels of calcium ions by fluorescing. GCaMP8 proteins consist of a transmembrane calcium-binding domain , bound to a peptide that modifies the activity of calmodulin. Two linkers attach calmodulin to a modified form of green fluorescent protein .
Despite the potential of these calcium sensors, early versions of GCaMP were hampered by issues such as poor response kinetics, low calcium sensitivity and limited correlation with the electrical activity of neurons. Initial versions of the sensors could detect only large changes in Cabrought about by tens of action potentials, with response kinetics on the order of several hundred milliseconds.
Considerable effort has since been dedicated to improving the performance of GCaMP sensors through structure-guided design. Later versions of GCaMP have even been optimized for sensitivity or speed, with ‘slow’ variants maximizing signal strength, and ‘fast’ variants maximizing response kinetics. Fast variants of GCaMP can now detect changes in calcium in time frames of tens of milliseconds.
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