Evidence map›Paper›PMID 26442584›Full record

ArticleThe Journal of biological chemistry2015

Cell Cycle-dependent Changes in Localization and Phosphorylation of the Plasma Membrane Kv2.1 K+ Channel Impact Endoplasmic Reticulum Membrane Contact Sites in COS-1 Cells.

Melanie M Cobb, Daniel C Austin, Jon T Sack, James S Trimmer

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. The Electrically Silent Kv5.1 Subunit Forms Heteromeric Kv2 Channels in Cortical Neurons and Confers Distinct Functional Properties.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Kv2.1 channels play opposing roles in regulating membrane potential, CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Review
  9. The tarantula toxin GxTx detains KThe Journal of general physiology · 2019
    Article
  10. Review
  11. Article
  12. Article
  13. Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. ER-plasma membrane junctions: Why and how do we study them?Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  17. Article
  18. Article
  19. Disruption of KNeuroscience · 2017
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Melanie M CobbFrom the Departments of Neurobiology, Physiology, and Behavior.
Daniel C AustinPhysiology and Membrane Biology, and.
Jon T SackPhysiology and Membrane Biology, and Anesthesiology and Pain Medicine, University of California Davis School of Medicine, Davis, California 95616.
James S TrimmerFrom the Departments of Neurobiology, Physiology, and Behavior, Physiology and Membrane Biology, and jtrimmer@ucdavis.edu.
University of California, Davis · US

Funding

Determinants of Dendritic Potassium Channel LocalizationR01NS042225 · NINDS · UNIVERSITY OF CALIFORNIA DAVIS · PI TRIMMER, JAMES S · 2001 to 2014
$6.3M
NINDS NIH HHS R01 NS042225
6 · The paper itself

Abstract

The plasma membrane (PM) comprises distinct subcellular domains with diverse functions that need to be dynamically coordinated with intracellular events, one of the most impactful being mitosis. The Kv2.1 voltage-gated potassium channel is conditionally localized to large PM clusters that represent specialized PM:endoplasmic reticulum membrane contact sites (PM:ER MCS), and overexpression of Kv2.1 induces more exuberant PM:ER MCS in neurons and in certain heterologous cell types. Localization of Kv2.1 at these contact sites is dynamically regulated by changes in phosphorylation at one or more sites located on its large cytoplasmic C terminus. Here, we show that Kv2.1 expressed in COS-1 cells undergoes dramatic cell cycle-dependent changes in its PM localization, having diffuse localization in interphase cells, and robust clustering during M phase. The mitosis-specific clusters of Kv2.1 are localized to PM:ER MCS, and M phase clustering of Kv2.1 induces more extensive PM:ER MCS. These cell cycle-dependent changes in Kv2.1 localization and the induction of PM:ER MCS are accompanied by increased mitotic Kv2.1 phosphorylation at several C-terminal phosphorylation sites. Phosphorylation of exogenously expressed Kv2.1 is significantly increased upon metaphase arrest in COS-1 and CHO cells, and in a pancreatic β cell line that express endogenous Kv2.1. The M phase clustering of Kv2.1 at PM:ER MCS in COS-1 cells requires the same C-terminal targeting motif needed for conditional Kv2.1 clustering in neurons. The cell cycle-dependent changes in localization and phosphorylation of Kv2.1 were not accompanied by changes in the electrophysiological properties of Kv2.1 expressed in CHO cells. Together, these results provide novel insights into the cell cycle-dependent changes in PM protein localization and phosphorylation.

Indexed as

Cell CycleAnimalsCell MembraneChlorocebus aethiopsCHO CellsCOS CellsCricetulusCytoplasmEndoplasmic ReticulumHEK293 CellsHumansInsulin-Secreting CellsMicroscopy, FluorescenceMitosisNeuronsPhosphorylationKcnb1 protein, ratShab Potassium Channelsendoplasmic reticulum (ER)membrane structuremitosisplasma membranepotassium channelprotein phosphorylationsubcellular organelle

Identifiers

PMID26442584
PMCPMC4705925
OpenAlexW2265043179

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.