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GKAP, a Novel Synaptic Protein That Interacts with the Guanylate Kinase-like Domain of the PSD-95/SAP90 Family of Channel Clustering Molecules
- Eunjoon Kim, S. Naisbitt, M. Sheng
- Biology, ChemistryJournal of Cell Biology
- 10 February 1997
The isolation of a novel synaptic protein, termed GKAP for guanylate kinase-associated protein, that binds directly to the GK domain of the four known members of the mammalian PSD-95 family, shows a unique domain structure and appears to be a major constituent of the postsynaptic density.
Competitive binding of α-actinin and calmodulin to the NMDA receptor
- M. Wyszynski, Jerry W. Lin, M. Sheng
- Biology, ChemistryNature
- 30 January 1997
The mechanisms by which neurotransmitter receptors are immobilized at postsynaptic sites in neurons are largely unknown. The activity of NMDA (N-methyl-D-aspartate) receptors is mechanosensitive1 and…
Heterogeneity in the Molecular Composition of Excitatory Postsynaptic Sites during Development of Hippocampal Neurons in Culture
- A. Rao, Eunjoon Kim, M. Sheng, A. Craig
- BiologyJournal of Neuroscience
- 15 February 1998
The results suggest that synapse development proceeds by formation of a postsynaptic scaffold containing PSD-95 and GKAP in concert with presynaptic vesicle clustering, followed by regulated attachment of glutamate receptor subtypes to this scaffold.
Competitive binding of alpha-actinin and calmodulin to the NMDA receptor.
- M. Wyszynski, J. Lin, M. Sheng
- Biology, ChemistryNature
- 1997
The mechanisms by which neurotransmitter receptors are immobilized at postsynaptic sites in neurons are largely unknown. The activity of NMDA (N-methyl-D-aspartate) receptors is mechanosensitive and…
Mismatched Appositions of Presynaptic and Postsynaptic Components in Isolated Hippocampal Neurons
- A. Rao, Eric M. Cha, A. Craig
- BiologyThe Journal of Neuroscience
- 15 November 2000
The results suggest the involvement of a synaptogenic signal common to glutamate and GABA synapses that permits experimentally induced mismatching of presynaptic and postsynaptic components in isolated neurons, as well as a second specificity-conferring signal that mediates appropriate matching in mixed cultures.
Differential Regional Expression and Ultrastructural Localization of α-Actinin-2, a Putative NMDA Receptor-Anchoring Protein, in Rat Brain
- M. Wyszynski, V. Kharazia, M. Sheng
- BiologyJournal of Neuroscience
- 15 February 1998
It is shown that α-actinin-2 is localized specifically in glutamatergic synapses in cultured hippocampal neurons and appropriately positioned at the ultrastructural level to function as a postsynaptic-anchoring protein for NMDA receptors.
Rapid Synaptic Remodeling by Protein Kinase C: Reciprocal Translocation of NMDA Receptors and Calcium/Calmodulin-Dependent Kinase II
- D. Fong, A. Rao, F. T. Crump, A. Craig
- Biology, ChemistryJournal of Neuroscience
- 15 March 2002
Positive activation of protein kinase C with phorbol esters induces a rapid dispersal of NMDA receptors from synaptic to extrasynaptic plasma membrane in cultured rat hippocampal neurons, revealing a surprisingly dynamic nature to the molecular composition and functional properties of glutamatergic postsynaptic specializations.
Characterization of Guanylate Kinase-Associated Protein, a Postsynaptic Density Protein at Excitatory Synapses That Interacts Directly with Postsynaptic Density-95/Synapse-Associated Protein 90
- S. Naisbitt, E. Kim, M. Sheng
- BiologyThe Journal of Neuroscience
- 1 August 1997
GKAP is a widely expressed neuronal protein localized specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
Evidence that protein constituents of postsynaptic membrane specializations are locally synthesized: analysis of proteins synthesized within synaptosomes
- A. Rao, O. Steward
- Biology, ChemistryJournal of Neuroscience
- 1 September 1991
The hypothesis that some synaptic proteins are locally synthesized at postsynaptic sites is supported by the evaluation of synaptosome fractions that included fragments of dendrites to incorporate labeled amino acid into protein.
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