Evidence map›Paper›PMID 18768923›Full record

ArticleAmerican journal of physiology. Cell physiology2008

Ankyrin facilitates intracellular trafficking of alpha1-Na+-K+-ATPase in polarized cells.

Paul R Stabach, Prasad Devarajan, Michael C Stankewich, Serguei Bannykh, Jon S Morrow

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  5. Functional compartmentalization of photoreceptor neurons.Pflugers Archiv : European journal of physiology · 2021
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  19. Targeted deletion of betaIII spectrin impairs synaptogenesis and generates ataxic and seizure phenotypes.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  20. Review
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.

Paul R StabachDept. of Pathology, Yale Univ., 310 Cedar St., New Haven, CT 06520, USA.
Prasad Devarajan
Michael C Stankewich
Serguei Bannykh
Jon S Morrow
Yale University · US

Funding

UNCONVENTIONAL MYOSINS IN RENAL FUNCTIONSP01DK055389 · NIDDK · YALE UNIVERSITY · PI MORROW, JON S · 1999 to 2004
$4.9M
MEMBRANE SKELETAL CONTROL IN HEMOLYTIC DISORDERSR01HL028560 · NHLBI · YALE UNIVERSITY · PI MORROW, JON S · 1985 to 2011
$3.3M
Topographic Spectrin Assembly in the Renal Tubule CellR01DK043812 · NIDDK · YALE UNIVERSITY · PI MORROW, JON S · 1991 to 2007
$1.9M
NHLBI NIH HHS R01-HL-28560NIDDK NIH HHS P01-DK-55389NIDDK NIH HHS R01-DK-43812
6 · The paper itself

Abstract

Defects in ankyrin underlie many hereditary disorders involving the mislocalization of membrane proteins. Such phenotypes are usually attributed to ankyrin's role in stabilizing a plasma membrane scaffold, but this assumption may not be accurate. We found in Madin-Darby canine kidney cells and in other cultured cells that the 25-residue ankyrin-binding sequence of alpha(1)-Na(+)-K(+)-ATPase facilitates the entry of alpha(1),beta(1)-Na(+)-K(+)-ATPase into the secretory pathway and that replacement of the cytoplasmic domain of vesicular stomatitis virus G protein (VSV-G) with this ankyrin-binding sequence bestows ankyrin dependency on the endoplasmic reticulum (ER) to Golgi trafficking of VSV-G. Expression of the ankyrin-binding sequence of alpha(1)-Na(+)-K(+)-ATPase alone as a soluble cytosolic peptide acts in trans to selectively block ER to Golgi transport of both wild-type alpha(1)-Na(+)-K(+)-ATPase and a VSV-G fusion protein that includes the ankyrin-binding sequence, whereas the trafficking of other proteins remains unaffected. Similar phenotypes are also generated by small hairpin RNA-mediated knockdown of ankyrin R or the depletion of ankyrin in semipermeabilized cells. These data indicate that the adapter protein ankyrin acts not only at the plasma membrane but also early in the secretory pathway to facilitate the intracellular trafficking of alpha(1)-Na(+)-K(+)-ATPase and presumably other selected proteins. This novel ankyrin-dependent assembly pathway suggests a mechanism whereby hereditary disorders of ankyrin may be manifested as diseases of membrane protein ER retention or mislocalization.

Indexed as

Ankyrin RepeatCell PolarityAnimalsAnkyrinsChlorocebus aethiopsCOS CellsCytoplasmDogsEndoplasmic ReticulumGolgi ApparatusHumansMembrane GlycoproteinsMonomeric GTP-Binding ProteinsProtein ConformationProtein FoldingProtein Sorting SignalsANK1 protein, humanANK3 protein, humanAnkyrinsATP1A1 protein, humanAtp1a1 protein, ratG protein, vesicular stomatitis virusMembrane GlycoproteinsMonomeric GTP-Binding ProteinsProtein Sorting SignalsRecombinant Fusion ProteinsRNA, Small InterferingSodium-Potassium-Exchanging ATPaseViral Envelope Proteins

Identifiers

PMID18768923
PMCPMC2584975
OpenAlexW1976823756

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.