Evidence map›Paper›PMID 15795311›Full record

ArticleThe Journal of general physiology2005

Mechanism of the voltage sensitivity of IRK1 inward-rectifier K+ channel block by the polyamine spermine.

Hyeon-Gyu Shin, Zhe Lu

Open access · greenAbstract read
In one paragraph

Article in The Journal of general physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Polyamine block of MthK potassium channels.The Journal of general physiology · 2020
    Article
  4. Article
  5. Article
  6. Polyamines and potassium channels: A 25-year romance.The Journal of biological chemistry · 2018
    Review
  7. External KThe Journal of general physiology · 2018
    Article
  8. Article
  9. Article
  10. Article
  11. Initial steps of inactivation at the K+ channel selectivity filter.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Functional consequences of Kir2.1/Kir2.2 subunit heteromerization.Pflugers Archiv : European journal of physiology · 2010
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Hyeon-Gyu ShinDepartment of Physiology, University of Pennsylvania, Philadelphia 19104, USA.
Zhe Lu
University of Pennsylvania · US

Funding

Permeation of Inward Rectifier K+ ChannelsR01GM055560 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LU, ZHE · 1997 to 2024
$8.4M
NIGMS NIH HHS GM55560NIGMS NIH HHS R01 GM055560
6 · The paper itself

Abstract

IRK1 (Kir2.1) inward-rectifier K+ channels exhibit exceedingly steep rectification, which reflects strong voltage dependence of channel block by intracellular cations such as the polyamine spermine. On the basis of studies of IRK1 block by various amine blockers, it was proposed that the observed voltage dependence (valence approximately 5) of IRK1 block by spermine results primarily from K+ ions, not spermine itself, traversing the transmembrane electrical field that drops mostly across the narrow ion selectivity filter, as spermine and K+ ions displace one another during channel block and unblock. If indeed spermine itself only rarely penetrates deep into the ion selectivity filter, then a long blocker with head groups much wider than the selectivity filter should exhibit comparably strong voltage dependence. We confirm here that channel block by two molecules of comparable length, decane-bis-trimethylammonium (bis-QA(C10)) and spermine, exhibit practically identical overall voltage dependence even though the head groups of the former are much wider ( approximately 6 A) than the ion selectivity filter ( approximately 3 A). For both blockers, the overall equilibrium dissociation constant differs from the ratio of apparent rate constants of channel unblock and block. Also, although steady-state IRK1 block by both cations is strongly voltage dependent, their apparent channel-blocking rate constant exhibits minimal voltage dependence, which suggests that the pore becomes blocked as soon as the blocker encounters the innermost K+ ion. These findings strongly suggest the existence of at least two (potentially identifiable) sequentially related blocked states with increasing numbers of K+ ions displaced. Consequently, the steady-state voltage dependence of IRK1 block by spermine or bis-QA(C10) should increase with membrane depolarization, a prediction indeed observed. Further kinetic analysis identifies two blocked states, and shows that most of the observed steady-state voltage dependence is associated with the transition between blocked states, consistent with the view that the mutual displacement of blocker and K+ ions must occur mainly as the blocker travels along the long inner pore.

Indexed as

Models, BiologicalAnimalsCells, CulturedComputer SimulationDose-Response Relationship, DrugHumansIon Channel GatingMembrane PotentialsOocytesPolyaminesPotassium Channels, Inwardly RectifyingSpermineXenopus laevisKCNJ2 protein, humanPolyaminesPotassium Channels, Inwardly RectifyingSpermine

Identifiers

PMID15795311
PMCPMC2217510
OpenAlexW2116242834

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.