FRET-FLIM investigation of PSD95-NMDA receptor interaction in dendritic spines; control by calpain, CaMKII and Src family kinase

Little is known about the changes in protein interactions inside synapses during synaptic remodeling, as their live monitoring in spines has been limited. We used a FRET-FLIM approach in developing cultured rat hippocampal neurons expressing fluorescently tagged NMDA receptor (NMDAR) and PSD95, two...

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Veröffentlicht in:	PloS one 2014-11, Vol.9 (11), p.e112170-e112170
Hauptverfasser:	Doré, Kim, Labrecque, Simon, Tardif, Christian, De Koninck, Paul
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biology and Life Sciences Ca2+/calmodulin-dependent protein kinase II Calcium-Calmodulin-Dependent Protein Kinase Type 2 - physiology Calpain Calpain - physiology Cells, Cultured Dendritic spines Dendritic Spines - enzymology Dendritic Spines - metabolism Dendritic Spines - physiology Developmental stages Disks Large Homolog 4 Protein Fluorescence Resonance Energy Transfer Glutamic acid receptors (ionotropic) HEK293 Cells Hippocampus Humans Inhibition Intracellular Signaling Peptides and Proteins - metabolism Kinases Membrane Proteins - metabolism N-Methyl-D-aspartic acid receptors Neuronal Plasticity - physiology Neurons Neurosciences Phosphorylation Postsynaptic density proteins Protein interaction Proteins Rats Receptors, N-Methyl-D-Aspartate - metabolism Remodeling Research and Analysis Methods Rodents Separation Signal Transduction Spine Src protein src-Family Kinases - physiology Synapses Synaptic plasticity
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