Functional and Molecular Aspects of Voltage‐Gated K+ Channel β Subunits

@article{Pongs1999FunctionalAM,
  title={Functional and Molecular Aspects of Voltage‐Gated K+ Channel $\beta$ Subunits},
  author={Olaf Pongs and Thorsten Leicher and Michaela Berger and Jochen Roeper and Robert B{\"a}hring and Dennis Wray and Karl Peter Giese and Alcino J. Silva and Johan Frederik Storm},
  journal={Annals of the New York Academy of Sciences},
  year={1999},
  volume={868}
}
ABSTRACT: Voltage‐gated potassium channels (Kv) of the Shaker‐related superfamily are assembled from membrane‐integrated α subunits and auxiliary β subunits. The β subunits may increase Kv channel surface expression and/or confer A‐type behavior to noninactivating Kv channels in heterologous expression systems. The interaction of Kvα and Kvβ subunits depends on the presence or absence of several domains including the amino‐terminal N‐type inactivating and NIP domains and the Kvα and Kvβ binding… 
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TLDR
It is concluded that the Kv4 channel complex employs novel alternative mechanisms of closed-state inactivation and the intracellular Zn2+ site in the T1 domain undergoes a conformational change tightly coupled to voltage-dependent gating and is targeted by nitrosative modulation.
Diverse roles for auxiliary subunits in phosphorylation-dependent regulation of mammalian brain voltage-gated potassium channels
TLDR
The complex effects of auxiliary subunits and phosphorylation provide a potent mechanism to generate additional diversity in the structure and function of Kv4 and Kv1 channels, as well as allowing for dynamic reversible regulation of these important ion channels.
Modulation of Kv4-encoded K+ Currents in the Mammalian Myocardium by Neuronal Calcium Sensor-1*
TLDR
The experiments reported here demonstrate that the neuronal calcium sensor protein-1 (NCS-1), another member of the recoverin-neuronal calcium sensor superfamily, is expressed in adult mouse ventricles and that NCS-1 co-immunoprecipitates with Kv4.3 from (adult mouse) ventricular extracts.
In vivo analysis of Kvβ2 function in Xenopus embryonic myocytes
TLDR
The results suggest that Kv1 potassium channel complexes in vivo have a strong requirement for both α and β subunits.
Kvβ Subunit Oxidoreductase Activity and Kv1 Potassium Channel Trafficking*
TLDR
It is found that all Kvβ subunits promote cell surface expression of coexpressed Kv1.2 α subunits in transfected COS-1 cells, which suggests that NADP+ binding and/or the integrity of the binding pocket structure, but not catalytic activity, of Kv β subunits is required for intracellular trafficking of K v1 channel complexes in mammalian cells and for axonal targeting in neurons.
Accessory Kv&bgr;1 Subunits Differentially Modulate the Functional Expression of Voltage-Gated K+ Channels in Mouse Ventricular Myocytes
TLDR
It is demonstrated that Kv&bgr;1 differentially regulates the functional cell surface expression of myocardial Ito,f and IK,slow2 channels.
Structure and function of Kv4-family transient potassium channels.
TLDR
A surprisingly large number of ancillary subunits and scaffolding proteins that can interact with the primary subunits of Shal-type K(+) channels, resulting in alterations in channel trafficking and kinetic properties are described.
Oxidation of NADPH on Kvβ1 inhibits ball-and-chain type inactivation by restraining the chain
TLDR
It is shown that after oxidation, the core domain binds to part of the N terminus, thus restraining it from blocking the channel, and establishes Kvβ as a target for pharmacological control of Kv1 channels.
The sigma‐1 receptor behaves as an atypical auxiliary subunit to modulate the functional characteristics of Kv1.2 channels expressed in HEK293 cells
TLDR
In transiently transfected HEK293 cells, it is found that ligand activation of the Sig‐1R modulates Kv1.2 current amplitude, and data suggest that Kvβ2 occludes the interaction of Sig-1R with Kv 1.2, and that E102 may be a residue critical for Sig‐ 1R modulation of Kv2.2 activation.
Kv1.1 and Kv1.2: Similar channels, different seizure models
TLDR
Voltage‐gated ion channels clustered in specific locations may present a novel therapeutic target for influencing excitability in neurologic disorders associated with some channelopathies.
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