Evidence map›Paper›PMID 37125772›Full record

ArticleAmerican journal of physiology. Cell physiology2023

The exocyst complex is required for the trafficking and delivery of KCa3.1 to the basolateral membrane of polarized epithelia.

Matthew J E Logue, Rachel E Farquhar, Yoakim Eckhoff-Björngard, Tanya T Cheung, Daniel C Devor, Fiona J McDonald, Kirk L Hamilton

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 77% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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 at 2 institutions in 2 countries.

Matthew J E LogueDepartment of Physiology, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Rachel E FarquharDepartment of Physiology, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Yoakim Eckhoff-BjörngardDepartment of Physiology, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Tanya T CheungDepartment of Physiology, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Daniel C DevorDepartment of Cell Biology, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.ORCID 0000-0003-3013-5179
Fiona J McDonaldDepartment of Physiology, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.ORCID 0000-0001-9242-166X
Kirk L HamiltonDepartment of Physiology, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.ORCID 0000-0003-1842-4023
University of Otago · NZUniversity of Pittsburgh · US

Funding

Assembly and Trafficking of IK1 and SK3 in EndotheliaR01HL092157 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI DEVOR, DANIEL C · 2009 to 2012
$1.5M
NHLBI NIH HHS R01 HL092157
6 · The paper itself

Abstract

Control of the movement of ions and water across epithelia is essential for homeostasis. Changing the number or activity of ion channels at the plasma membrane is a significant regulator of epithelial transport. In polarized epithelia, the intermediate-conductance calcium-activated potassium channel, KCa3.1 is delivered to the basolateral membrane where it generates and maintains the electrochemical gradients required for epithelial transport. The mechanisms that control the delivery of KCa3.1 to the basolateral membrane are still emerging. Herein, we investigated the role of the highly conserved tethering complex exocyst. In epithelia, exocyst is involved in the tethering of post-Golgi secretory vesicles with the basolateral membrane, which is required before membrane fusion. In our Fisher rat thyroid cell line that stably expresses KCa3.1, siRNA knockdown of either of the exocyst subunits Sec3, Sec6, or Sec8 significantly decreased KCa3.1-specific current. In addition, knockdown of exocyst complex subunits significantly reduced the basolateral membrane protein level of KCa3.1. Finally, co-immunoprecipitation experiments suggest associations between Sec6 and KCa3.1, but not between Sec8 and KCa3.1. Collectively, based on these data and our previous studies, we suggest that components of exocyst complex are crucially important in the tethering of KCa3.1 to the basolateral membrane. After which,

Indexed as

Epithelial CellsMembrane FusionAnimalsCell MembraneEpitheliumRatsSNARE ProteinsSNARE ProteinsexocystIK1KCa3.1KCNN4SK4trafficking

Identifiers

PMID37125772
PMCPMC10243536
OpenAlexW4367600819

What Socratic 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 Socratic graph.