Evidence map›Paper›PMID 9380700›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin-ankyrin G119 skeleton in Madin Darby canine kidney cells.

P Devarajan, P R Stabach, M A De Matteis, J S Morrow

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Salt-induced NaPflugers Archiv : European journal of physiology · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Actin acting at the Golgi.Histochemistry and cell biology · 2013
    Review
  15. Regulation of the cardiac sodium pump.Cellular and molecular life sciences : CMLS · 2013
    Review
  16. Article
  17. Article
  18. Spectrin-based skeleton as an actor in cell signaling.Cellular and molecular life sciences : CMLS · 2012
    Review
  19. Review
  20. 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
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

4 authors at 2 institutions in 2 countries.

P DevarajanDepartment of Pediatrics, Yale University, New Haven, CT 06520, USA. prasad.devarajan@yale.edu
P R Stabach
M A De Matteis
J S Morrow
Mario Negri Sud Foundation · ITYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spectrin (betaISigma*) and ankyrin (AnkG119) associate with Golgi membranes and the dynactin complex, but their role in vesicle trafficking remains uncertain. We find that the actin-binding domain and membrane-association domain 1 (MAD1) of betaI spectrin together form a constitutive Golgi targeting signal in transfected MDCK cells. Expression of this signal in transfected cells disrupts the endogenous Golgi spectrin skeleton and blocks transport of alpha- and beta-Na,K-ATPase and vesicular stomatitis virus-G protein from the endoplasmic reticulum (ER) but does not disrupt the formation of Golgi stacks, the distribution of beta-COP, or the transport and surface display of E-cadherin. The Golgi spectrin skeleton is thus required for the transport of a subset of membrane proteins from the ER to the Golgi. We postulate that together with polyfunctional adapter proteins such as AnkG119, Golgi spectrin forms a docking complex that acts prior to the cis-Golgi, presumably with vesicular-tubular clusters (VTCs or ERGIC), to sequester specific membrane proteins into vesicles transiting between the ER and Golgi, and subsequently (probably involving other isoforms of spectrin and ankyrin) to mediate cargo transport within the Golgi and to other membrane compartments. We hypothesize that this vesicular spectrin-ankyrin adapter-protein trafficking (or tethering) system (SAATS) mediates the capture and transport of many membrane proteins and acts in conjunction with vesicle-targeting molecules to effect the efficient transport of cargo proteins.

Indexed as

AnimalsAnkyrinsBiological TransportCell LineDogsEndoplasmic ReticulumGolgi ApparatusHumansKidneyProtein Sorting SignalsSodium-Potassium-Exchanging ATPaseSpectrinTransfectionAnkyrinsProtein Sorting SignalsSodium-Potassium-Exchanging ATPaseSpectrin

Identifiers

PMID9380700
PMCPMC23456
OpenAlexW2038376484

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.