Abstract
S100 Ca2+-binding proteins have been associated with a multitude of intracellular Ca2+-dependent functions including regulation of the cell cycle, cell differentiation, cell motility and apoptosis, modulation of membrane–cytoskeletal interactions, transduction of intracellular Ca2+ signals, and in mediating learning and memory. S100 proteins are fine tuned to read the intracellular 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.
Highlights
Ion channel proteins form hydrophilic pores integrated into lipid bilayer membranes allowing the passage of ions into and out of cells
Many ion channels are highly selective for a certain type of ion, such as K+, Na+, Ca2+, or Cl−; others, like N -methyl-d-aspartate (NMDA) or α-amino-3-hydroxy-5-methyl-4isoxazolepropionic acid receptor (AMPA) receptors, are less selective and allow different cations to pass
protein soluble in 100% ammonium sulfate (S100) proteins from a vertebrate host have the potential to interact with binding sites on channels or to modulate intracellular signaling to an extent that channel gating is affected in an invading non-vertebrate organism
Summary
Ion channel proteins form hydrophilic pores integrated into lipid bilayer membranes allowing the passage of ions into and out of cells. A number of ion channels are activated or modulated by intracellular Ca2+ signals giving rise to the notion that Ca2+ binding proteins (CaBP) may play a role in regulating channel gating function.
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