Visualization of Na,K-ATPase interacting proteins using FRET technique.
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.
Uhlén
Per
P
Department of Woman and Child Health, Karolinska Intitutet, Astrid Lindgren Children's Hospital, S-171 76, Stockholm, Sweden. per.uhlen@kbh.ki.se
D000818:Animals; D002118:Calcium / Q000502:physiology; D020013:Calcium Signaling / Q000502:physiology*; D002352:Carrier Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004735:Energy Transfer; D007150:Immunohistochemistry; D016297:Mutagenesis, Site-Directed; D010042:Ouabain / Q000494:pharmacology; D017354:Point Mutation; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013050:Spectrometry, Fluorescence / Q000379:methods
D002352:Carrier Proteins; D010042:Ouabain; D000254:Sodium-Potassium-Exchanging ATPase; D002118:Calcium