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Cells of the heart contain a variety of calcium-transporting proteins that play an important role in the regulation of intracellular calcium concentrations (Ca2+). The inward-rectifying Ca2+-ATPase (IACa) is a prototypical plasma membrane Ca2+-transporting protein that operates in a two-step process to pump Ca2+ from the cytosol into the extracellular fluid. The first step, effected by the ‘flippase’ component of the IACa, is characterised by the breakdown of a phospholipid, PIP2, to generate a lipid, PIP. The second step, effected by the ‘hydrophobic chain’ component of the IACa, is characterised by the translocation of Ca2+ and/or PIP from the plasma membrane to the cytoplasm, a process driven by a component of the IACa termed the Ca-pumping ATPase. Recent studies using novel direct measurements of the membrane potential have demonstrated that (1) IACa pumps Ca2+ and not PIP2 across the plasma membrane, and (2) the hydrolysis of ATP by IACa is coupled to the translocation of a Ca2+ ion, not PIP, from the membrane to the cytosol. Here, using a new formulation of the radial diffusion model to represent the relationship between the generation and translocation of Ca2+ from the plasma membrane to the cytosol, and steady-state studies using novel fluorescent Ca2+ indicators, we show that the translocation
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