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Additional recommended knowledge
Dephosphorylated phospholamban interacts with the Ca2+ ATPase pump (SERCA) to lower its activity and sensitivity to Ca2+, thus decreasing Ca2+ uptake into the sarcoplasmic reticulum (SR). Phospholamban is phosphorylated by Protein Kinase A, inducing an order-to-disorder transition, activating the SERCA. Thus, when phospholamban is phosphorylated, its interaction with SERCA is reduced, resulting in an increase in Ca2+ transport into the SR.
Because phospholamban is a substrate for PKA, which is activated with beta-adrenergic stimulation, one would expect relaxation to be favored when PKA is activated. However, this also means that more Ca2+ is stored in the SR and thus more is available for release; this would increase contractility.
Gene knockout of phospholamban results in animals with hyperdynamic hearts, with little apparent negative consequence.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Phospholamban". A list of authors is available in Wikipedia.|