Evidence map›Paper›PMID 26424804›Full record

ArticleMolecular biology of the cell2015

Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin.

Glen A Farr, Michael Hull, Emily H Stoops, Rosalie Bateson, Michael J Caplan

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. On the existence of endocytosis driven by membrane phase separations.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  3. Article
  4. Single-molecule labeling for studying trafficking of renal transporters.American journal of physiology. Renal physiology · 2018
    Review
  5. Review
  6. Article
  7. 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

5 authors at 1 institution in 1 country.

Glen A FarrDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026.
Michael HullDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026.
Emily H StoopsDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026.
Rosalie BatesonDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026.
Michael J CaplanDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026 michael.caplan@yale.edu).
Yale University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
The Regulation of Renal Epithelial Cell Junction Assembly and PolarizationP01DK017433 · NIDDK · YALE UNIVERSITY · PI FORBUSH, BLISS · 1986 to 2018
$29.5M
Pathways and Partners in Renal Epithelial Cell PolarityR01DK072614 · NIDDK · YALE UNIVERSITY · PI CAPLAN, MICHAEL J. · 2005 to 2022
$6.9M
NIDDK NIH HHS DK072612NIDDK NIH HHS DK17433NIDDK NIH HHS P01 DK017433NIDDK NIH HHS R01 DK072614NIGMS NIH HHS 5T32GM007223-35NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Recent evidence indicates that newly synthesized membrane proteins that share the same distributions in the plasma membranes of polarized epithelial cells can pursue a variety of distinct trafficking routes as they travel from the Golgi complex to their common destination at the cell surface. In most polarized epithelial cells, both the Na,K-ATPase and E-cadherin are localized to the basolateral domains of the plasma membrane. To examine the itineraries pursued by newly synthesized Na,K-ATPase and E-cadherin in polarized MDCK epithelial cells, we used the SNAP and CLIP labeling systems to fluorescently tag temporally defined cohorts of these proteins and observe their behaviors simultaneously as they traverse the secretory pathway. These experiments reveal that E-cadherin is delivered to the cell surface substantially faster than is the Na,K-ATPase. Furthermore, the surface delivery of newly synthesized E-cadherin to the plasma membrane was not prevented by the 19 °C temperature block that inhibits the trafficking of most proteins, including the Na,K-ATPase, out of the trans-Golgi network. Consistent with these distinct behaviors, populations of newly synthesized E-cadherin and Na,K-ATPase become separated from one another within the trans-Golgi network, suggesting that they are sorted into different carrier vesicles that mediate their post-Golgi trafficking.

Indexed as

AnimalsCadherinsCell AdhesionCell MovementCells, CulturedDogsEpithelial CellsFluorescent Antibody TechniqueGolgi ApparatusMadin Darby Canine Kidney CellsMicroscopyProtein TransportSecretory PathwaySodium-Potassium-Exchanging ATPasetrans-Golgi NetworkCadherinsSodium-Potassium-Exchanging ATPase

Identifiers

PMID26424804
PMCPMC4666135
OpenAlexW2221044769

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.