Evidence map›Paper›PMID 14711382›Full record

ArticleBMC physiology2004

Heterotrimeric G protein subunits are located on rat liver endosomes.

Rebecca W Van Dyke

Open access · bronzeAbstract read
In one paragraph

Article in BMC physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Components of the GTraffic (Copenhagen, Denmark) · 2020
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. G protein trafficking.Sub-cellular biochemistry · 2012
    Review
  11. Review
  12. Review
  13. Article
  14. A specific role of AGS3 in the surface expression of plasma membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  15. An obligatory requirement for the heterotrimeric G protein Gi3 in the antiautophagic action of insulin in the liver.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  16. 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

1 author at 1 institution in 1 country.

Rebecca W Van DykeDept of Internal Medicine, University of Michigan School of Medicine and Veterans Administration Hospital, Ann Arbor, MI 48105, USA. wynne@umich.edu
University of Michigan–Ann Arbor · US

Funding

LIVER PROTON AND SOLUTE TRANSPORT AND ENDOCYTOSISR01DK038333 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VAN DYKE, REBECCA W. · 1988 to 1997
–
NIDDK NIH HHS R01 DK38333
6 · The paper itself

Abstract

backgroundRat liver endosomes contain activated insulin receptors and downstream signal transduction molecules. We undertook these studies to determine whether endosomes also contain heterotrimeric G proteins that may be involved in signal transduction from G protein-coupled receptors.

resultsBy Western blotting Gsalpha, Gialpha1,2, Gialpha3 and Gbeta were enriched in both canalicular (CM) and basolateral (BLM) membranes but also readily detectable on three types of purified rat liver endosomes in the order recycling receptor compartment (RRC) > compartment for uncoupling of receptor and ligand (CURL) > multivesicular bodies (MVB) >> purified secondary lysosomes. Western blotting with antibodies to Na, K-ATPase and to other proteins associated with plasma membranes and intracellular organelles indicated this was not due to contamination of endosome preparations by CM or BLM. Adenylate cyclase (AC) was also identified on purified CM, BLM, RRC, CURL and MVB. Percoll gradient fractionation of liver postnuclear supernatants demonstrated co-occurrence of endosomes and heterotrimeric G protein subunits in fractions with little plasma membrane markers. By confocal microscopy, punctate staining for Gsalpha, Gialpha3 and Gbeta corresponded to punctate areas of endocytosed Texas red-dextran in hepatocytes from control and cholera toxin-treated livers.

conclusionWe conclude that heterotrimeric G protein subunits as well as AC likely traffic into hepatocytes on endosome membranes, possibly generating downstream signals spatially separate from signalling generated at the plasma membrane, analogous to the role(s) of internalized insulin receptors.

Indexed as

Adenylyl CyclasesAnimalsBlotting, WesternCholera ToxinEndocytosisEndosomesHepatocytesHeterotrimeric GTP-Binding ProteinsLysosomesMaleMicroscopy, ConfocalMicroscopy, FluorescenceRatsRats, Sprague-DawleyReceptors, G-Protein-CoupledSignal TransductionAdenylyl CyclasesCholera ToxinHeterotrimeric GTP-Binding ProteinsReceptors, G-Protein-Coupled

Identifiers

PMID14711382
PMCPMC324412
OpenAlexW1609540500

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.