Differential K+ Channel Clustering Activity of PSD-95 and SAP97, Two Related Membrane-associated Putative Guanylate Kinases

@article{Kim1996DifferentialKC,
  title={Differential K+ Channel Clustering Activity of PSD-95 and SAP97, Two Related Membrane-associated Putative Guanylate Kinases},
  author={E. Kim and Morgan Sheng},
  journal={Neuropharmacology},
  year={1996},
  volume={35},
  pages={993-1000}
}
Psd-95 and Sap97 Exhibit Distinct Mechanisms for Regulating K+ Channel Surface Expression and Clustering
TLDR
Data show that ion channel clustering by PSD-95 and SAP97 occurs by distinct mechanisms, and suggests that these channel-clustering proteins may play diverse roles in regulating the abundance and distribution of channels at synapses and other neuronal membrane specializations.
Ion Channel Clustering by Membrane-associated Guanylate Kinases
TLDR
The data suggest that lipid modifications and heavy metal associations with the N termini of MAGUKs mediate differential functions and subcellular localizations of these synaptic scaffolds.
GKAP, a Novel Synaptic Protein That Interacts with the Guanylate Kinase-like Domain of the PSD-95/SAP90 Family of Channel Clustering Molecules
TLDR
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.
Cell Surface Targeting and Clustering Interactions between Heterologously Expressed PSD-95 and the Shal Voltage-gated Potassium Channel, Kv4.2*
TLDR
This work represents the first evidence that a member of the Shal subfamily of Kv channels can bind to PSD-95, with functional consequences, in the heterologous expression system.
Distinct Structural Requirements for Clustering and Immobilization of K+ Channels by PSD-95
TLDR
Fluorescence recovery after photobleaching showed that PSD-95 can immobilize K+ channels in the plasma membrane in an all-or-none manner, and the structural requirements for protein clustering and immobilization by PSd-95 are distinct.
Clustering of neuronal potassium channels is independent of their interaction with PSD-95
TLDR
Surprisingly, it is found that the high density clustering of Kv1 channels and Caspr2 at juxtaparanodes is normal in a mutant mouse lacking juxtaparanodal PSD-95, and that the indirect interaction between Kv 1 channels andCaspr2 is maintained in these mutant mice.
Requirement of N-terminal Cysteines of PSD-95 for PSD-95 Multimerization and Ternary Complex Formation, but Not for Binding to Potassium Channel Kv1.4*
TLDR
It is suggested that the N-terminal cysteine residues are essential for PSD-95 multimerization and thatMultimerization is required for simultaneous binding of multiple membrane protein ligands by PSd-95.
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References

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TLDR
Functional and biochemical evidence is presented that cell-surface clustering of Shaker-subfamily K+ channels is mediated by the PSD-95 family of membrane-associated putative guanylate kinases, and the ability of PDZ domains to function as independent modules for protein–protein interaction, and their presence in other junction-associated molecules suggest that PDZ-domain-containing polypeptides may be widely involved in the organization of proteins at sites of membrane specialization.
Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
  • M. Niethammer, E. Kim, M. Sheng
  • Biology, Chemistry
    The Journal of neuroscience : the official journal of the Society for Neuroscience
  • 1996
TLDR
Data suggest that PDZ domains can function as modules for protein-protein interactions and members of the PSD-95 family might serve to anchor NMDA receptors to the submembrane cytoskeleton and aid in the assembly of signal transduction complexes at postsynaptic sites.
Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein
TLDR
Light and immunoelectron microscopic analysis of the rat hippocampal formation revealed that SAP97 is localized in the presynaptic nerve termini of excitatory synapses, suggesting that members of the SAP90/SAP97 subfamily may be involved in the site specific assembly, stability or functions of membrane specialization at sites of cell-cell contact.
Association and colocalization of K+ channel alpha- and beta-subunit polypeptides in rat brain
TLDR
The results suggest that neuronal mechanisms may exist to direct the selective interaction of K+ channel alpha- and beta- subunit polypeptides, and that the properties of K- channels in specific subcellular domains may be regulated by the formation of heteromultimeric K- channel complexes containing specific combinations of alpha-and-subunits.
Contrasting subcellular localization of the Kv1.2 K+ channel subunit in different neurons of rat brain
TLDR
The findings suggest that Kv1.2-containing K+ channels may play diverse functional roles in several neuronal compartments, regulating presynaptic or postsynaptic membrane excitability, depending on the neuronal cell type.
Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
TLDR
The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95, which may affect the plasticity of excitatory synapses.
Presynaptic A-current based on heteromultimeric K+ channels detected in vivo
A WIDE variety of voltage-gated K+ channels are involved in the regulation of neuronal excitability and synaptic transmission. Their heterogeneity arises in part from the large number of genes
Localization of Kv1.1 and Kv1.2, two K channel proteins, to synaptic terminals, somata, and dendrites in the mouse brain
TLDR
It is shown that two closely related voltage- gated potassium channel proteins, mKv1.1 and mKV1.2, are present in multiple subcellular locations including cell somata, juxta-paranodal regions of myelinated axons, synaptic terminals, unmyelinatedAxons, specialized junctions among axon, and proximal dendrites.
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