Toward understanding the assembly and structure of KATP channels.

@article{AguilarBryan1998TowardUT,
  title={Toward understanding the assembly and structure of KATP channels.},
  author={Lydia Aguilar-Bryan and John P. Clement and G Gonz{\'a}lez and Kumud Kunjilwar and Andrey P. Babenko and Joseph Bryan},
  journal={Physiological reviews},
  year={1998},
  volume={78 1},
  pages={
          227-45
        }
}
Adenosine 5'-triphosphate-sensitive potassium (KATP) channels couple metabolic events to membrane electrical activity in a variety of cell types. The cloning and reconstitution of the subunits of these channels demonstrate they are heteromultimers of inwardly rectifying potassium channel subunits (KIR6.x) and sulfonylurea receptors (SUR), members of the ATP-binding cassette (ABC) superfamily. Recent studies indicate that SUR and KIR6.x associate with 1:1 stoichiometry to assemble a large… 
A view of sur/KIR6.X, KATP channels.
TLDR
Understanding the mutations in SUR and KIR6.X is allowing insight into how these channels respond to nucleotides, sulfonylureas, and potassium channel openers, KCOs.
ATP-sensitive potassium channels: a model of heteromultimeric potassium channel/receptor assemblies.
  • S. Seino
  • Biology, Medicine
    Annual review of physiology
  • 1999
TLDR
KATP channels are the first example of a heteromultimeric complex assembled with a K+ channel and a receptor that are structurally unrelated to each other.
Molecular biology of adenosine triphosphate-sensitive potassium channels.
TLDR
The results indicate that SUR1 is important in sensing nucleotide changes, as implied by its sequence similarity to other ABC proteins, in addition to being the drug sensor, and the inhibitory action of ATP appears to be through a site located on KIR6.2, whose affinity for ATP is modified by SUR1.
Production and purification of ATP-sensitive potassium channel particles for cryo-electron microscopy.
TLDR
A method for expressing KatP channels in mammalian cell culture, solubilizing the channel in detergent micelles and purifying KATP channels using an affinity tag to the SURx subunit for cryoEM structural studies is described.
ATP-sensitive potassium channels: structures, functions, and pathophysiology.
TLDR
The functional diversity of the various KATP channels is being determined by a combination of the Kir6.0 subunit and the SUR subunit comprising it, a new model in which ABC proteins regulate the functional expression of ion channels.
KATP channels gated by intracellular nucleotides and phospholipids.
TLDR
The mechanisms and molecular determinants that underlie gating of KATP channel by nucleotides and phospholipids and their physiological implications are discussed.
Structure of a Pancreatic ATP-Sensitive Potassium Channel
TLDR
A molecular mechanism for KATP regulation by anti-diabetic sulfonylurea drugs, intracellular adenosine nucleotide concentrations, and PIP2 lipid is suggested.
The Carboxyl Termini of KATP Channels Bind Nucleotides*
TLDR
The COOH termini of KATPtetrameric channels contain the nucleotide-binding pockets of these metabolically regulated channels with four potential nucleotide -binding sites/channel tetramer.
Trafficking motifs in potassium channels
TLDR
Investigation of the previously unknown mechanisms of biosynthetic and endosomal trafficking of the KATP and hERG potassium channels concluded that these processes play an important role in maintaining surface density and thereby in the function of these channels in physiological and patho-physiological conditions.
Assembly Limits the Pharmacological Complexity of ATP-sensitive Potassium Channels*
TLDR
It is concluded that heteromultimeric channel complexes containing both SUR1 and SUR2A are not formed, suggesting an incompatibility between different SUR subtypes, which limits the pharmacological complexity of K ATP channels that may be observed in native tissues.
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References

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Reconstitution of IKATP: An Inward Rectifier Subunit Plus the Sulfonylurea Receptor
TLDR
Gene mapping data indicate that these pancreatic β cell potassium channels are a complex composed of at least two subunits-BIR, a member of the inward rectifier potassium channel family, and SUR, a members of the ATP-binding cassette superfamily.
A Family of Sulfonylurea Receptors Determines the Pharmacological Properties of ATP-Sensitive K+ Channels
TLDR
The present study shows that the ATP sensitivity and pharmacological properties of K(ATP) channels are determined by a family of structurally related but functionally distinct sulfonylurea receptors.
Association and Stoichiometry of KATP Channel Subunits
ATP-sensitive potassium channels (K(ATP) channels) are heteromultimers of sulfonylurea receptors (SUR) and inwardly rectifying potassium channel subunits (K(IR)6.x) with a (SUR-K(IR)6.x)4
Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor
TLDR
It is shown that the primary site at which ATP acts to mediate K-ATP channel inhibition is located on Kir6.2, and that SUR1 is required for sensitivity to sulphonylureas and diazoxide and for activation by Mg-ADP.
A Novel Sulfonylurea Receptor Forms with BIR (Kir6.2) a Smooth Muscle Type ATP-sensitive K+ Channel*
TLDR
The reverse transcription-polymerase chain reaction analysis showed that mRNA of this clone was ubiquitously expressed in diverse tissues, including brain, heart, liver, urinary bladder, and skeletal muscle, suggesting that this novel isoform of sulfonylurea receptor is a subunit reconstituting the smooth muscle KATP channel.
Determination of the subunit stoichiometry of an inwardly rectifying potassium channel
TLDR
It is found that IRK1 channels, like voltage-gated K+ channels, are tetrameric channels, and the high sensitivity to Mg2+ and polyamines, cations that produce inward rectification by blocking the channel pore from the cytoplasmic side is largely retained in a channel containing only one wild-type subunit and three subunits bearing mutations that abolish high affinity Mg 2+ andpolyamine block.
Sulphonylurea receptor 2B and Kir6.1 form a sulphonylurea‐sensitive but ATP‐insensitive K+ channel.
TLDR
The K+ channel composed of the sulphonylurea receptor 2B and an inwardly rectifying K+Channel subunit Kir6.1 is not a classical ATP‐sensitive K+channel but closely resembles the nucleotide diphosphate‐dependent K+ channels in vascular smooth muscle cells.
Adenosine 5'-triphosphate-sensitive potassium channels.
  • F. Ashcroft
  • Biology, Medicine
    Annual review of neuroscience
  • 1988
TLDR
The close correlation between cell metabolism and the activity of the ATP-sensitive K-channel raises the intriguing possibility that disorders of cell metabolism might produce alterations in channel activity and consequent changes in cell function.
Cloning, Tissue Expression, and Chromosomal Localization of SUR2, the Putative Drug-Binding Subunit of Cardiac, Skeletal Muscle, and Vascular KATP Channels
TLDR
The isolation of cDNAs encoding SUR-like proteins from mouse, SUR2A and SUR2B are described and the structure of the predicted protein and expression pattern of SUR2 suggests that it is the drug-binding channel-modulating subunit of the extrapancreatic KATP channel.
Anionic Phospholipids Activate ATP-sensitive Potassium Channels*
TLDR
Metabolism of anionic phospholipids in plasmalemmal membrane may be a novel and general mechanism for regulation of KATP and perhaps other ion channels in the family of inward rectifiers.
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