S100 Ca+-bindingproteins have been associated with a multitude of intracellular Ca+dependent functions including regulation of the cellc ycle, celldifferentiation, cell motility and apoptosis, modulation ofmembrane-cytoskeletal interactions,transduction of intracellular Ca2+ signals, and in mediating learning and memory. S100 proteins are fine tuned to read thei ntracellular free Ca2+ concentration and affect protein phosphorylation, which makes them candidates to modulate certain ion channels and neuronal electrical behavior. Certain S100s are secreted from cells and are found in extracellular fluids where they exert unique extracellular functions. In addition to their neurotrophic activity, some S100 proteins modulate neuronal electrical discharge activity and appear to act directly on ion channels. The first reports regarding these effects suggested S100-mediated alterations in Ca2+ fluxes, K+ currents, and neuronal discharge activity. Recent reports revealed direct and indirect interactions with Ca2+, K+, Cl−, and ligand activated channels. This review focuses on studies of the physical and functional interactions of S100 proteins and ion channels.
S100 Calcium-Binding Proteins and Ion Channels
DONATO, Rosario Francesco;
2012
Abstract
S100 Ca+-bindingproteins have been associated with a multitude of intracellular Ca+dependent functions including regulation of the cellc ycle, celldifferentiation, cell motility and apoptosis, modulation ofmembrane-cytoskeletal interactions,transduction of intracellular Ca2+ signals, and in mediating learning and memory. S100 proteins are fine tuned to read thei ntracellular free Ca2+ concentration and affect protein phosphorylation, which makes them candidates to modulate certain ion channels and neuronal electrical behavior. Certain S100s are secreted from cells and are found in extracellular fluids where they exert unique extracellular functions. In addition to their neurotrophic activity, some S100 proteins modulate neuronal electrical discharge activity and appear to act directly on ion channels. The first reports regarding these effects suggested S100-mediated alterations in Ca2+ fluxes, K+ currents, and neuronal discharge activity. Recent reports revealed direct and indirect interactions with Ca2+, K+, Cl−, and ligand activated channels. This review focuses on studies of the physical and functional interactions of S100 proteins and ion channels.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
