A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of α‐actinin‐2

@article{Cukovic2001ADA,
  title={A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of $\alpha$‐actinin‐2},
  author={Daniela Cukovic and Grace W K Lu and Barbara A. Wible and David F. Steele and David Fedida},
  journal={FEBS Letters},
  year={2001},
  volume={498}
}
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N‐terminal PDZ‐binding domain in Kv1 potassium channels
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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.
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A specific N-terminal residue in Kv1.5 is required for upregulation of the channel by SAP97.
Role for Myosin-V Motor Proteins in the Selective Delivery of Kv Channel Isoforms to the Membrane Surface of Cardiac Myocytes
TLDR
To investigate the role of the unconventional myosin-V (MYO5A and MYO5B) motors in determining the cell surface density of Kv1.5, it is shown that these isoform-specific trafficking pathways determine Kv 1.5-encoded IKur in myocytes to regulate repolarizing current and, consequently, cardiac excitability.
The Spectrin Cytoskeleton Influences the Surface Expression and Activation of Human Transient Receptor Potential Channel 4 Channels*
TLDR
Results demonstrate that a direct interaction between h TRPC4 and the spectrin cytoskeleton is involved in the regulation of hTRPC4 surface expression and activation.
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.
Modulation of voltage sensitivity by N-terminal cytoplasmic residues in human Kv1.2 channels
TLDR
The data imply that N-terminal residues can interact with transmembrane regions and perturb the machinery mediating voltage-dependent channel gating, as well as constructing chimæras from the collection of human voltage-gated potassium channels.
Modulation of Kv1.5 currents by protein kinase A, tyrosine kinase, and protein tyrosine phosphatase requires an intact cytoskeleton.
TLDR
It is concluded that currents encoded by Kv1.5 are regulated by PKA and protein tyrosine phosphatase and that this regulation requires an intact actin cytoskeleton and alpha-actinin-2.
KChIP2 modulates the cell surface expression of Kv 1.5-encoded K(+) channels.
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References

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α‐Actinin‐2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells
Interactions of Calmodulin and α-Actinin with the NR1 Subunit Modulate Ca2+-Dependent Inactivation of NMDA Receptors
TLDR
It is proposed that inactivation can occur after C0 dissociates from α-actinin by two distinct but converging calcium-dependent processes: competitive displacement ofα-act inin by calmodulin and reduction in the affinity of α-Actinin for C0 after binding of calcium to α- actinin.
An α-Actinin Binding Site of Zyxin Is Essential for Subcellular Zyxin Localization and α-Actinin Recruitment*
TLDR
It is demonstrated that human zyxin, like the avian protein, specifically interacts with α-actinin, and the interaction site is mapped to a motif of approximately 22 amino acids, present in the N-terminal domain of humanZyxin.
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TLDR
It is reported that the alpha-actinin-binding region of CRP is confined to an 18-residue sequence occurring within the protein's N-terminal glycine-rich repeat, revealing the critical importance of a single lysine residue (lysine 65 in human CRP1).
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Competitive binding of α-actinin and calmodulin to the NMDA receptor
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…
Stilbenes and fenamates rescue the loss of IKS channel function induced by an LQT5 mutation and other IsK mutants
TLDR
It is shown that binding of IKS channel activators, such as stilbenes and fenamates, to an extracellular domain flanking the human IsK transmembrane segment, restores normal I KS channel gating in otherwise inactive IsK C‐terminal mutants, including the naturally occurring LQT5 mutant, D76N.
Differential K+ Channel Clustering Activity of PSD-95 and SAP97, Two Related Membrane-associated Putative Guanylate Kinases
Binding of ADAM12, a Marker of Skeletal Muscle Regeneration, to the Muscle-specific Actin-binding Protein, α-Actinin-2, Is Required for Myoblast Fusion*
TLDR
It is shown that ADAM12 is dramatically up-regulated in regenerated, newly formed fibers in vivo and suggests that interaction of ADAM 12 with α-actinin-2 is important forADAM12 function.
Evolution of the spectrin repeat
TLDR
This analysis shows how a modular protein unit can be used in the evolution of large cytoskeletal structures by concluding that spectrin evolved from α‐actinin by an elongation process that included two duplications of a block of seven repeats.
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