Evidence map›Paper›PMID 11069304›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Apical sorting of a voltage- and Ca2+-activated K+ channel alpha -subunit in Madin-Darby canine kidney cells is independent of N-glycosylation.

M Bravo-Zehnder, P Orio, A Norambuena, M Wallner, P Meera, L Toro, R Latorre, A González

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Cholesterol, PtdIns(4,5)PbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Regulation of potassium channel trafficking in the distal nephron.Current opinion in nephrology and hypertension · 2013
    Review
  11. Stiffened lipid platforms at molecular force foci.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Cholesterol and ion channels.Sub-cellular biochemistry · 2010
    Review
  18. Review
  19. Article
  20. 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

8 authors at 1 institution in 1 country.

M Bravo-ZehnderDepartamento de Inmunologia Clinica y Reumatologia, Facultad de Medicina, Departamento de Biologia Celular y Molecular, Pontificia Universidad Católica de Chile, Santiago.
P Orio
A Norambuena
M Wallner
P Meera
L Toro
R Latorre
A González
Millennium Institute for Integrative Biology · CL

Funding

STRUCTURAL DETERMINANTS OF K(CA) CHANNEL FUNCTIONR01HL054970 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORO DE STEFANI, LIGIA G. · 1995 to 2009
$3.2M
NHLBI NIH HHS HL54970NHLBI NIH HHS R01 HL054970
6 · The paper itself

Abstract

The voltage- and Ca(2+)-activated K(+) (K(V,Ca)) channel is expressed in a variety of polarized epithelial cells seemingly displaying a tissue-dependent apical-to-basolateral regionalization, as revealed by electrophysiology. Using domain-specific biotinylation and immunofluorescence we show that the human channel K(V,Ca) alpha-subunit (human Slowpoke channel, hSlo) is predominantly found in the apical plasma membrane domain of permanently transfected Madin-Darby canine kidney cells. Both the wild-type and a mutant hSlo protein lacking its only potential N-glycosylation site were efficiently transported to the cell surface and concentrated in the apical domain even when they were overexpressed to levels 200- to 300-fold higher than the density of intrinsic Slo channels. Furthermore, tunicamycin treatment did not prevent apical segregation of hSlo, indicating that endogenous glycosylated proteins (e.g., K(V,Ca) beta-subunits) were not required. hSlo seems to display properties for lipid-raft targeting, as judged by its buoyant distribution in sucrose gradients after extraction with either detergent or sodium carbonate. The evidence indicates that the hSlo protein possesses intrinsic information for transport to the apical cell surface through a mechanism that may involve association with lipid rafts and that is independent of glycosylation of the channel itself or an associated protein. Thus, this particular polytopic model protein shows that glycosylation-independent apical pathways exist for endogenous membrane proteins in Madin-Darby canine kidney cells.

Indexed as

Potassium Channels, Calcium-ActivatedAnimalsCalciumCell LineCell MembraneCentrifugation, Density GradientDogsGlycosylationHumansKidneyLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMutagenesis, Site-DirectedPatch-Clamp TechniquesPotassium ChannelsCalciumLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsPotassium ChannelsPotassium Channels, Calcium-ActivatedProtein SubunitsRecombinant Proteins

Identifiers

PMID11069304
PMCPMC27187
OpenAlexW2008312998

What OpenQuestion holds

Textmetadata
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.