Nanodisc-based kinetic assays reveal distinct effects of phospholipid headgroups on the phosphoenzyme transition of sarcoplasmic reticulum Ca²⁺-ATPase.

ABSTRACT: Sarco(endo)plasmic reticulum Ca²⁺-ATPase catalyzes ATP-driven Ca²⁺ transport from the cytoplasm to the lumen and is critical for a range of cell functions, including muscle relaxation. Here, we investigated the effects of the headgroups of the 1-palmitoyl-2-oleoyl glycerophospholipids phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylserine (PS), and phosphatidylglycerol (PG) on sarcoplasmic reticulum (SR) Ca²⁺-ATPase embedded into a nanodisc, a lipid-bilayer construct harboring the specific lipid. We found that Ca²⁺-ATPase activity in a PC bilayer is comparable with that of SR vesicles and is suppressed in the other phospholipids, especially in PS. Ca²⁺ affinity at the high-affinity transport sites in PC was similar

SUBMITTER: Yamasaki K 

PROVIDER: S-EPMC5724008 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature