Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases

@article{Kim1995ClusteringOS,
  title={Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases},
  author={Eunjoon Kim and Martin Niethammer and Adam Rothschild and Yuh Nung Jan and Morgan Sheng},
  journal={Nature},
  year={1995},
  volume={378},
  pages={85-88}
}
ANCHORING of ion channels at specific subcellular sites is critical for neuronal signalling, but the mechanisms underlying channel localization and clustering are largely unknown (reviewed in ref. 1). Voltage-gated K+ channels are concentrated in various neuronal domains, including presynaptic terminals, nodes of Ranvier and dendrites, where they regulate local membrane excitability. Here we present functional and biochemical evidence that cell-surface clustering of Shaker-subfamily K+ channels… 
Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins
TLDR
The results suggest that the C-terminal domain of the Shaker Kv channel behaves as an entropic chain and support a “fishing rod” molecular mechanism for KV channel binding to scaffold proteins.
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.
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.
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.
Intrinsically disordered C-terminal segments of voltage-activated potassium channels: a possible fishing rod-like mechanism for channel binding to scaffold proteins
TLDR
It is demonstrated that the C-terminal segments of Kv channels adjacent to the PDZ-binding motif are intrinsically disordered, and this indicates an inter-molecular fishing rod-like mechanism for K(+) channel binding to scaffold proteins.
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.
Association of Neuronal Calcium Channels with Modular Adaptor Proteins*
TLDR
This work demonstrates a specific association of the cytosolic carboxyl terminus of the N-type Ca2+ channel pore-forming α1B subunit with the modular adaptor proteins Mint1 and CASK and advances the understanding of coupling between cell adhesion and synaptic vesicle exocytosis.
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