Abstract
Phospholemman (FXYD1, or PLM) is a key regulator of Na+-K+ ATPase in the heart, and is principally phosphorylated by cAMP-dependent protein kinase A (PKA) and protein kinase C (PKC). To investigate whether phosphorylation alters FXYD1 structure and oligomerization, we fused cyan or yellow fluorescent protein (CFP/YFP) to the c-terminus of FXYD1 and co-expressed the fusion proteins in AAV-293 cells. Phosphorylation of FXYD1 was mimicked by mutations S68E (PKA site) or S63E/S68E (PKC+PKA sites), and FRET from CFP-FXYD1 to YFP-FXYD1 was quantified by acceptor photobleaching.
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