You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Ca2+/calmodulin-kinase II Enhances Channel Conductance of α -amino-3-hydroxy-5-methyl-4-isoxazolepropionate Type Glutamate Receptors
Victor Derkach, Andres Barria and Thomas R. Soderling
Proceedings of the National Academy of Sciences of the United States of America
Vol. 96, No. 6 (Mar. 16, 1999), pp. 3269-3274
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/47525
Page Count: 6
You can always find the topics here!Topics: Long term potentiation, Receptors, Phosphorylation, Neurons, Inurement, Pipettes, Electric current, Membrane potential, Time constants, Glutamate receptors
Were these topics helpful?See something inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
The ability of central glutamatergic synapses to change their strength in response to the intensity of synaptic input, which occurs, for example, in long-term potentiation (LTP), is thought to provide a cellular basis for memory formation and learning. LTP in the CA1 field of the hippocampus requires activation of Ca2+/calmodul II (CaM-KII), which phosphorylates Ser-831 in the GluR1 subunit of the α -amino-3-hydroxy-5-methyl-4-isoxazolepropionate glutamate receptor (AMPA-R), and this activation/phosphorylation is thought to be a postsynaptic mechanism in LTP. In this study, we have identified a molecular mechanism by which CaM-KII potentiates AMPA-Rs. Coexpression in HEK-293 cells of activated CaM-KII with GluR1 did not affect the glutamate affinity of the receptor, the kinetics of desensitization and recovery, channel rectification, open probability, or gating. Single-channel recordings identified multiple conductance states for GluR1, and coexpression with CaM-KII or a mutation of Ser-831 to Asp increased the contribution of the higher conductance states. These results indicate that CaM-KII can mediate plasticity at glutamatergic synapses by increasing single-channel conductance of existing functional AMPA-Rs or by recruiting new high-conductance-state AMPA-Rs.
Proceedings of the National Academy of Sciences of the United States of America © 1999 National Academy of Sciences