SERCA resides in the sarcoplasmic reticulum (SR) within muscle cells. It is a Ca2+ ATPase which transfers Ca2+ from the cytosol of the cell to the lumen of the SR at the expense of ATP hydrolysis during muscle relaxation.
SERCA is normally somewhat inhibited by a protein, phospholamban, with which it is closely associated. Another protein, calsequestrin, binds calcium within the SR and helps to reduce the concentration of free calcium within the SR, which assists SERCA so that it does not have to pump against such a high concentration gradient. The SR has a much higher concentration of Ca2+ (10,000x) inside when compared to the intracellular Ca2+ concentration.
The rate at which SERCA moves Ca2+ across the SR membrane can be controlled by phospholamban (PLB/PLN) under ß-adrenergic stimulation. When PLB is associated with SERCA, the rate of Ca2+ movement is reduced, upon dissociation of PLB Ca2+ movement increases.
There are 3 major paralogs, SERCA1-3, which are expressed at various levels in different cell types.
There are additional post-translational isoforms of both SERCA2 and 3 which serve to introduce the possibility of cell type specific Ca2+-reuptake responses as well as increasing the overall complexity of the Ca2+ signalling mechanism.
- Sarcoplasmic+Reticulum+Calcium-Transporting+ATPases at the US National Library of Medicine Medical Subject Headings (MeSH)
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