N‐terminal PDZ‐binding domain in Kv1 potassium channels

@article{Eldstrom2002NterminalPD,
  title={N‐terminal PDZ‐binding domain in Kv1 potassium channels},
  author={Jodene Eldstrom and Kyle W Doerksen and David F. Steele and David Fedida},
  journal={FEBS Letters},
  year={2002},
  volume={531}
}
The role of the T1 domain in the trafficking of Kv1.5
The T1 domain of Kv channels is important in the subfamily-specific assembly by clustering individual monomers to increase their chances of interaction into tetramers. Furthermore, T1 domain plays
Kif5b is an essential forward trafficking motor for the Kv1.5 cardiac potassium channel
TLDR
Kif5b is essential to anterograde trafficking of a cardiac voltage‐gated potassium channel, and the dominant negative acts by indirectly inhibiting endocytosis.
The C-Terminal PDZ-Binding Motif in the Kv1.5 Potassium Channel Governs its Modulation by the Na+/H+ Exchanger Regulatory Factor 2
TLDR
The results suggest that NHERFs might participate in the regulation of electrical excitability in part by controlling Kv1.5 surface abundance and by clustering signal transduction molecules to the channel.
Interactions between the C-terminus of Kv1.5 and Kvβ regulate pyridine nucleotide-dependent changes in channel gating
TLDR
Pull-down experiments, structural analysis and electrophysiological data indicated that a specific region of the C-terminus is required for Kvβ binding and that this interaction is essential for the differential regulation of Kv currents by oxidized and reduced nucleotides.
A specific N-terminal residue in Kv1.5 is required for upregulation of the channel by SAP97.
Localization of Kv1.5 in native and heterologous cell systems
TLDR
A detailed characterization of antibodies and expression of Kvl .5 in canine cardiac tissue unambiguously demonstrated a physiological role for the channel expressed in the atria and contributing to the repolarization phase of the atrial action potential.
Tetramerization domain mutations in KCNA5 affect channel kinetics and cause abnormal trafficking patterns.
TLDR
Immunostaining data support the hypothesis that, while WT protein localizes to the plasma membrane, mutant protein is mainly retained in intracellular packets, and a role for the T1 domain in channel kinetics as well as in KCNA5 channel subcellular localization.
Post‐synaptic density perturbs insulin‐induced Kv1.3 channel modulation via a clustering mechanism involving the SH3 domain
The olfactory bulb (OB) contains the highest concentration of the insulin receptor (IR) kinase in the central nervous system; however, its functional role and modulation in this region remains poorly
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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.
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TLDR
The crystal structures of PDZ domains, with and without ligand, have been determined and demonstrate the mode of ligand‐binding and the structural bases for sequence conservation among diversePDZ domains.
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The PDZ protein interaction domain of neuronal nitric oxide synthase (nNOS) can heterodimerize with the PDZ domains of postsynaptic density protein 95 and syntrophin through interactions that are not
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TLDR
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TLDR
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TLDR
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TLDR
The identification and characterization of a new skeletal muscle protein containing a PDZ domain that binds to the COOH-terminal region of alpha-actinin-2 is reported, and this novel 31-kD protein is specifically expressed in heart and skeletal muscle.
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TLDR
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