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Visualization of Na,K‐ATPase Interacting Proteins Using FRET Technique
Author(s) -
UHLÉN PER
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2003.tb07237.x
Subject(s) - förster resonance energy transfer , endoplasmic reticulum , signal transduction , intracellular , biophysics , chemistry , lipid microdomain , calcium signaling , microbiology and biotechnology , atpase , fluorescence , membrane , biochemistry , enzyme , biology , physics , quantum mechanics
A bstract : Signaling transduction mediated by protein aggregates within specific microdomains has been receiving increased attention. We previously showed that Na,K‐ATPase, partially inhibited by ouabain, induces intracellular calcium (Ca 2+ ) oscillations which involve Ca 2+ release from the endoplasmic reticulum (ER). Plasma membrane bound Na,K‐ATPase and proteins in the ER are in close proximity to each other, and signal transduction may occur via a physical interaction or a microdomain. To study these signaling pathways and intricate microenvironments, sophisticated methods are required. One way to detect molecular interactions in the nanometer scale (1‐10 nm) is fluorescence resonance energy transfer (FRET). Thus, FRET provides vital insight into the action of Na,K‐ATPase to trigger intracellular signaling events.