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Signal transduction molecules at the glutamatergic postsynaptic membrane

Kennedy, Mary B. (1998) Signal transduction molecules at the glutamatergic postsynaptic membrane. Brain Research Reviews, 26 (2-3). pp. 243-257. ISSN 0165-0173. http://resolver.caltech.edu/CaltechAUTHORS:20120424-150822198

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Abstract

We have applied techniques from modern molecular biology and biochemistry to unravel the complex molecular structure of the postsynaptic membrane at glutamatergic synapses in the central nervous system. We have characterized a set of new proteins that are constituents of the postsynaptic density, including PSD-95, densin-180, citron (a rho/rac effector protein), and synaptic gp130 Ras GAP (a new Ras GTPase-activating protein). The structure of PSD-95 revealed a new protein motif, the PDZ domain, that plays an important role in the assembly of signal transduction complexes at intercellular junctions. More recently, we have used new imaging tools to observe the dynamics of autophosphorylation of CaM kinase II in intact hippocampal tissue. We have been able to detect changes in the amount of autophosphorylated CaM kinase II in dendrites, individual synapses, and somas of hippocampal neurons following induction of long-term potentiation by tetanic stimulation. In addition, we have observed a specific increase in the concentration of CaM kinase II in dendrites of neurons receiving tetanic stimulation. This increase appears to be the result of dendritic synthesis of new protein. Over the next several years we will apply similar methods to study regulatory changes that occur at the molecular level in glutamatergic synapses in the CNS as the brain processes and stores new information.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/S0165-0173(97)00043-XDOIUNSPECIFIED
http://www.sciencedirect.com/science/article/pii/S016501739700043XPublisherUNSPECIFIED
Additional Information:© 1998 Elsevier Science B.V. Available online 13 July 1998. I wish to thank all members of my laboratory who have performed the work discussed here, and acknowledge Jason Lee who provided Fig. 1, and Yannan Ouyang who provided Fig. 3. This work was supported by grants NS28710, NS17660, and training grant GMS07616 from the National Institutes of Health; grant MH49176 from the National Institute of Mental Health; grant GER-9023446 from NSF; and by funds from the Beckman Institute, Del-Webb and Merck Foundations.
Funders:
Funding AgencyGrant Number
NIHNS28710
NIHNS17660
NIH Training GrantGMS07616
National Institute of Mental HealthMH49176
NSFGER-9023446
Beckman InstituteUNSPECIFIED
Del-Webb FoundationUNSPECIFIED
Merck FoundationUNSPECIFIED
Subject Keywords:Postsynaptic density; Protein phosphorylation; Protein kinases; Ras; Rac; Long-term potentiation
Record Number:CaltechAUTHORS:20120424-150822198
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20120424-150822198
Official Citation:Mary B. Kennedy, Signal transduction molecules at the glutamatergic postsynaptic membrane, Brain Research Reviews, Volume 26, Issues 2–3, May 1998, Pages 243-257, ISSN 0165-0173, 10.1016/S0165-0173(97)00043-X.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:30312
Collection:CaltechAUTHORS
Deposited By: Melanie Stefan
Deposited On:25 Apr 2012 20:40
Last Modified:25 Apr 2012 20:40

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