title: AMPA receptors do the electric slide.
abstract: How the synapse is organized and how its organization changes during events that result in long-term changes in synaptic efficacy is the subject of intense study. Various anchoring proteins work in concert to organize the postsynaptic side of the membrane, and the interactions of these proteins can be altered by synaptic activity. DeSouza and Ziff discuss the evidence that the reversible palmitoylation of the postsynaptic density protein PSD-95 may result in the movement of AMPA-type glutamate receptors into and out of lipid raft domains, ultimately controlling AMPA receptor accumulation at the postsynaptic membrane.
authors.affiliation: Howard Hughes Medical Institute, Department of Biochemistry, New York University School of Medicine, New York, NY 10016, USA.
authors.forename: Sunita
authors.initials: S
authors.lastname: deSouza
authors.forename: Edward B
authors.initials: EB
authors.lastname: Ziff
mesh_terms: D018698:Glutamic Acid / Q000502:physiology; D021962:Membrane Microdomains / Q000502:physiology; D008565:Membrane Proteins / Q000502:physiology; D008954:Models, Biological; D018377:Neurotransmitter Agents / Q000502:physiology; D018091:Receptors, AMPA / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology; D013570:Synaptic Membranes / Q000502:physiology
chemical_list: D008565:Membrane Proteins; D018377:Neurotransmitter Agents; D018091:Receptors, AMPA; D018698:Glutamic Acid