Evidence map›Paper›PMID 8700891›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Inhibition of G-protein betagamma-subunit functions by phosducin-like protein.

S Schröder, M J Lohse

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

14 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structure of the thioredoxin-fold domain of human phosducin-like protein 2.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  10. Article
  11. Review
  12. The amyloid precursor protein interacts with Go heterotrimeric protein within a cell compartment specialized in signal transduction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    Article
  13. Article
  14. Phosducin is a ubiquitous G-protein regulator.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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

2 authors at 1 institution in 1 country.

S SchröderLaboratory of Molecular Biology, University of Munich, Germany.
M J Lohse
MRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosducin is a cytosolic protein predominantly expressed in the retina and the pineal gland that can interact with the betagamma subunits of guanine nucleotide binding proteins (G proteins) and thereby may regulate transmembrane signaling. A cDNA encoding a phosducin-like protein (PhLP) has recently been isolated from rat brain [Miles, M. F., Barhite, S., Sganga, M. & Elliott, M. (1993) Proc. Natl. Acad. Sci. USA 90, 10831-10835. Here we report the expression of PhLP in Escherichia coli and its purification. Recombinant purified PUP inhibited multiple effects of G-protein betagamma subunits. First, it inhibited the betagamma-subunit-dependent ADP-ribosylation of purified alpha(o) by pertussis toxin. Second, it inhibited the GTPase activity of purified G(o). The IC50 value of PhLP in the latter assay was 89 nM, whereas phosducin caused half-maximal inhibition at 17 nM. And finally, PhLP antagonized the enhancement of rhodopsin phosphorylation by purified betagamma subunits. The N terminus of PhLP shows no similarity to the much longer N terminus of phosducin, the region shown to be critical for phosducin-betagamma-subunit interactions. Therefore, PhLP appears to bind to G-protein betagamma subunits by an as yet unknown mode of interaction and may represent an endogenous regulator of G-protein function.

Indexed as

AnimalsBase SequenceCarrier ProteinsDNA PrimersEnzyme InhibitorsEye ProteinsGTP-Binding Protein RegulatorsGTP-Binding ProteinsGTP PhosphohydrolasesMolecular ChaperonesMolecular Sequence DataNerve Tissue ProteinsPertussis ToxinPhosphoproteinsPhosphorylationRatsCarrier ProteinsDNA PrimersEnzyme InhibitorsEye ProteinsGTP-Binding Protein RegulatorsGTP-Binding ProteinsGTP PhosphohydrolasesMolecular ChaperonesNerve Tissue ProteinsPdcl protein, ratPertussis ToxinphosducinPhosphoproteinsRecombinant ProteinsRhodopsinVirulence Factors, Bordetella

Identifiers

PMID8700891
PMCPMC39916
OpenAlexW1964634901

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.