Evidence map›Paper›PMID 18668522›Full record

ArticleJournal of cellular physiology2008

Multiple Kv1.5 targeting to membrane surface microdomains.

Ramón Martínez-Mármol, Núria Villalonga, Laura Solé, Rubén Vicente, Michael M Tamkun, Concepció Soler, Antonio Felipe

Abstract read
In one paragraph

Article in Journal of cellular physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Palmitoylation of Voltage-Gated Ion Channels.International journal of molecular sciences · 2022
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Voltage-dependent K(+)-channel responses during activation and damage in alveolar macrophages induced by quartz particles.Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban · 2009
    Article
  19. 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

7 authors.

Ramón Martínez-MármolMolecular Physiology Laboratory, Departament de Bioquímica i Biologia Molecular, Institut de Biomedicina, Universitat de Barcelona, Barcelona, Spain.
Núria Villalonga
Laura Solé
Rubén Vicente
Michael M Tamkun
Concepció Soler
Antonio Felipe

Funding

REGULATORY MECHANISMS OF CARDIAC REPOLARIZATIONR01HL049330 · NHLBI · VANDERBILT UNIVERSITY · PI TAMKUN, MICHAEL M. · 1993 to 2005
$2.1M
Targeting of Voltage-gated K+ Channels to Lipid RaftsR01NS041542 · NINDS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI TAMKUN, MICHAEL M. · 2001 to 2004
$1.5M
NHLBI NIH HHS HL49330NHLBI NIH HHS R01 HL049330NINDS NIH HHS NS41542NINDS NIH HHS R01 NS041542
6 · The paper itself

Abstract

Surface expression of voltage-dependent K(+) channels (Kv) has a pivotal role in leukocyte physiology. Although little is known about the physiological role of lipid rafts, these microdomains concentrate signaling molecules and their ion channel substrates. Kv1.3 associates with Kv1.5 to form functional channels in macrophages. Different isoform stoichiometries lead to distinct heteromeric channels which may be further modulated by targeting the complex to different membrane surface microdomains. Kv1.3 targets to lipid rafts, whereas Kv1.5 localization is under debate. With this in mind, we wanted to study whether heterotetrameric Kv1.5-containing channels target to lipid rafts. While in transfected HEK-293 cells, homo- and heterotetrameric channels targeted to rafts, Kv1.5 did not target to rafts in macrophages. Therefore, Kv1.3/Kv1.5 hybrid channels are mostly concentrated in non-raft microdomains. However, LPS-induced activation, which increases the Kv1.3/Kv1.5 ratio and caveolin, targeted Kv1.5 back to lipid rafts. Moreover, Kv1.5 did not localize to low-buoyancy fractions in L6E9 skeletal myoblasts, which also coexpress both channels, heart membranes or cardiomyocyes. Coexpression of a Cav3(DGV)-mutant confined Kv1.5 to Cav3(DGV)-vesicles of HEK cells. Contrarily, coexpression of Kvbeta2.1 impaired the Kv1.5 targeting to raft microdomains in HEK cells. Our results indicate that Kv1.5 partnership interactions are underlying mechanisms governing channel targeting to lipid rafts.

Indexed as

AnimalsCaveolin 3Cell LineCell SeparationCholesterolHumansKv1.3 Potassium ChannelKv1.5 Potassium ChannelMacrophagesMembrane MicrodomainsMiceMuscle, SkeletalMyocardiumMyocytes, CardiacProtein SubunitsProtein TransportCaveolin 3CholesterolKv1.3 Potassium ChannelKv1.5 Potassium ChannelProtein Subunits

Identifiers

PMID18668522
PMCPMC2577364

What OpenQuestion holds

Textmetadata
LicenceTDM
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.