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Cited by 197Ion channel regulation and functionPancreatic function and diabetesATP Synthase and ATPases Research

Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating

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Martin, Gregory M, Yoshioka, Craig, Rex, Emily A, Fay, Jonathan F, Xie, Qing, Whorton, Matthew R, Chen, James Z, Shyng, Show-Ling·2017·eLife
DOI 10.7554/elife.24149PMC PMC5344670

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Abstract

KATP channels are metabolic sensors that couple cell energetics to membrane excitability. In pancreatic β-cells, channels formed by SUR1 and Kir6.2 regulate insulin secretion and are the targets of antidiabetic sulfonylureas. Here, we used cryo-EM to elucidate structural basis of channel assembly and gating. The structure, determined in the presence of ATP and the sulfonylurea glibenclamide, at ~6 Å resolution reveals a closed Kir6.2 tetrameric core with four peripheral SUR1s each anchored to a Kir6.2 by its N-terminal transmembrane domain (TMD0). Intricate interactions between TMD0, the loop following TMD0, and Kir6.2 near the proposed PIP2 binding site, and where ATP density is observed, suggest SUR1 may contribute to ATP and PIP2 binding to enhance Kir6.2 sensitivity to both. The SUR1-ABC core is found in an unusual inward-facing conformation whereby the two nucleotide binding domains are misaligned along a two-fold symmetry axis, revealing a possible mechanism by which glibenclamide inhibits channel activity.

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  • The putative ATP-binding site of Kir6.2 sits at the interface between the N-terminus of one subunit and the C-terminus of the other, with the β-phosphate of ATP interacting with residue K185.

    “It sits at the interface between the N-terminus of one subunit and the C-terminus of the other, with the β-phosphate of ATP interacting with residue K185.”

    From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [432]

  • The KATP channel complex has SUR1 subunits arranged around a central tetrameric Kir6.2 pore.

    “The structure of the KATP channel complex reveals the SUR1 subunits are arranged around a central tetrameric Kir6.2 pore (393, 432, 450) (Figure 7B,C).”

    From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [432]

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Authors
Martin, G. M., Yoshioka, C., Rex, E. A., Fay, J. F., Xie, Q., Whorton, M. R., Chen, J. Z., & Shyng, S.-L.
Affiliations
Oregon Health & Science University (US)
Corresponding author
  • Chen, James Z
  • Shyng, Show-Ling
ORCID
Venue
eLife
Publisher
eLife Sciences Publications, Ltd
Published
2017-01-16
Volume
6
ISSN
2050-084X (ISSN-L)
DOI
10.7554/elife.24149
PMC
PMC5344670
OpenAlex
W2574882949
Cited by
197
References
78
Citations by year
2026: 9 · 2025: 10 · 2024: 17 · 2023: 19 · 2022: 12 · 2021: 27 · 2020: 24 · 2019: 23 · 2018: 29 · 2017: 27
FWCI
11.45
Type
journal article
Language
en
Open access
Licence
Locations
  • eLife (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK066485, F31DK105800)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords
ATP-sensitive potassium channels, Kir6.2, SUR1, sulfonylurea receptor, glibenclamide, channel gating, channel assembly, PIP2 binding, ATP binding, nucleotide-binding domain, inward-facing conformation, pancreatic beta cells, insulin secretion
MeSH terms
Kcnj11 Channel, Adenosine Triphosphate, Glyburide, Humans, Models, Molecular, Protein Conformation, Cryoelectron Microscopy, Potassium Channels, Inwardly Rectifying, Protein Multimerization, Sulfonylurea Receptors

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