Reference work entry
Sarcolipin (SLN) was first identified by David MacLennan in 1974 as a “proteolipid” in purified rabbit skeletal muscle sarcoplasmic reticulum (SR) preparations (MacLennan 1974). In 1992, Wawrzynow et al. determined its sequence, confirmed its molecular weight as 3,733 Da, and named it sarcolipin (SLN) with reference to its nature and origin (Wawrzynow et al. 1992). SLN protein sequence is highly conserved from fish to man. For nearly three decades, the exact function of SLN remained unknown. Early studies suggested that it is very similar to phospholamban (PLB), an important regulator of the SERCA pump in cardiac muscle (Fig. 1). Using reconstituted synthetic SLN and SERCA, Lee et al. first proposed the idea that SLN binding to SERCA could promote uncoupling of SERCA ATP hydrolysis from Ca 2+ transport (Mall et al. 2006). More recent studies from our laboratory have shown that SLN binding to SERCA causes uncoupling of SR Ca 2+transport from ATP...
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