Evidence map›Paper›PMID 18635543›Full record

ArticleThe Journal of biological chemistry2008

Phosphorylation and ankyrin-G binding of the C-terminal domain regulate targeting and function of the ammonium transporter RhBG.

Fabien Sohet, Yves Colin, Sandrine Genetet, Pierre Ripoche, Sylvain Métral, Caroline Le Van Kim, Claude Lopez

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Trial
  2. Rhbg interaction with CA-IV and its effects on NHAmerican journal of physiology. Cell physiology · 2025
    Article
  3. Chloride Gradient Is Involved in Ammonium Influx in Human Erythrocytes.International journal of molecular sciences · 2024
    Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Ammonia transport in the kidney by Rhesus glycoproteins.American journal of physiology. Renal physiology · 2014
    Review
  11. Article
  12. Article
  13. Article
  14. Molecular physiology of the Rh ammonia transport proteins.Current opinion in nephrology and hypertension · 2010
    Review
  15. 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

7 authors at 2 institutions in 1 country.

Fabien SohetINSERM, U665, Paris F-75015, the Institut National de la Transfusion Sanguine, 6 Rue Alexandre Cabanel, Paris F-75015, France.
Yves Colin
Sandrine Genetet
Pierre Ripoche
Sylvain Métral
Caroline Le Van Kim
Claude Lopez
Inserm · FRInstitut National de la Transfusion Sanguine · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RhBG, a human member of the Amt/Mep/Rh/superfamily of ammonium transporters, has been shown to facilitate NH(3) transport and to be anchored to the basolateral plasma membrane of kidney epithelial cells, via ankyrin-G. We showed here that triple alanine substitution of the (419)FLD(421) sequence, which links the cytoplasmic C-terminal domain of RhBG to ankyrin-G, not only disrupted the interaction of RhBG with the spectrin-based skeleton but also delayed its cell surface expression, decreased its plasma membrane stability, and abolished its NH(3) transport function in epithelial cell lines. Similarly, we demonstrated that both anchoring to the membrane skeleton and ammonium transport activity are regulated by the phosphorylation status of the C-terminal tail of RhBG. Tyrosine 429, which belongs to the previously reported YED basolateral targeting signal of RhBG, was demonstrated to be phosphorylated in vitro using purified Src and Syk kinases and ex vivo by analyzing the effect of pervanadate treatment on wild-type RhBG or Y429A mutants. Then, we showed that Y429D and Y429E mutations, mimicking constitutive phosphorylation, abolished NH(3) transport and enhanced Triton X-100 solubilization of RhBG from the cell membrane. In contrast, the nonphosphorylated/nonphosphorylatable Y429A and Y429F mutants behaved the same as wild-type RhBG. Conversely, Y/A or Y/F but not Y/E or Y/D mutations of residue 429 abolished the exclusive basolateral localization of RhBG in polarized epithelial cells. All these results led to a model in which targeting and ammonium transport function of RhBG are regulated by both phosphorylation and membrane skeleton binding of the C-terminal cytoplasmic domain.

Indexed as

Amino Acid SubstitutionAmmoniaAnimalsAnkyrinsCation Transport ProteinsCell LineCell MembraneCell PolarityCytoskeletonDogsEnzyme InhibitorsEpithelial CellsGlycoproteinsHumansIntracellular Signaling Peptides and ProteinsIon TransportAmmoniaANK3 protein, humanAnk3 protein, mouseAnkyrinsCation Transport ProteinsEnzyme InhibitorsGlycoproteinsIntracellular Signaling Peptides and ProteinsMembrane Transport ProteinspervanadateProtein-Tyrosine KinasesRHBG protein, humanRhBG protein, mouseSpectrinsrc-Family KinasesSyk KinaseSYK protein, humanSyk protein, mouseVanadates

Identifiers

PMID18635543
PMCPMC3258915
OpenAlexW2001511706

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.