Cytosolic PSD-95 interactor alters functional organization of neural circuits and AMPA receptor signaling independent of PSD-95 binding

• Published in: Network neuroscience (Cambridge, Mass.) Vol. 5; no. 1; pp. 166 - 197
• Main Authors: Rodriguez, Ana R., Anderson, Erin D., O’Neill, Kate M., McEwan, Przemyslaw P., Vigilante, Nicholas F., Kwon, Munjin, Akum, Barbara F., Stawicki, Tamara M., Meaney, David F., Firestein, Bonnie L.
• Format: Journal Article
• Language: English
• Published: One Rogers Street, Cambridge, MA 02142-1209, USA MIT Press 01.02.2021; MIT Press Journals, The; The MIT Press
• Subjects: AMPA receptors; Binding; Circuits; Clustering; Computational neuroscience; Cypin; Density; Electrophysiology; Firing rate; Functional morphology; Glutamic acid receptors; Glutamic acid receptors (ionotropic); Hippocampal neurons; Localization; Microelectrode array; Microelectrodes; Mutants; N-Methyl-D-aspartic acid receptors; Networks; Neural circuits; Neural networks; Postsynaptic density; Postsynaptic density proteins; Proteins; Receptor density; Receptors; Synapses; Synaptic density; Synaptosomes; Toxicity; Waveforms; α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid; α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors; Electrophysiology; Hippocampal neurons; Microelectrode array; AMPA receptors; Neural circuits; Cypin

Cytosolic PSD-95 interactor (cypin) regulates many aspects of neuronal development and function, ranging from dendritogenesis to synaptic protein localization. While it is known that removal of postsynaptic density protein-95 (PSD-95) from the postsynaptic density decreases synaptic N-methyl-D-aspar...