Evidence map›Paper›PMID 1378615›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

Tyrosine phosphorylation of G protein alpha subunits by pp60c-src.

W P Hausdorff, J A Pitcher, D K Luttrell, M E Linder, H Kurose, S J Parsons, M G Caron, R J Lefkowitz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Receptor tyrosine kinases activate heterotrimeric G proteins via phosphorylation within the interdomain cleft of Gαi.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Article
  6. Article
  7. Review
  8. Tyrosine phosphorylation switching of a G protein.The Journal of biological chemistry · 2018
    Article
  9. Article
  10. Article
  11. Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Posttranslational modification of Galphao1 generates Galphao3, an abundant G protein in brain.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  18. Article
  19. Article
  20. The association between glycosylphosphatidylinositol-anchored proteins and heterotrimeric G protein alpha subunits in lymphocytes.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

8 authors at 1 institution in 1 country.

W P HausdorffHoward Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710.
J A Pitcher
D K Luttrell
M E Linder
H Kurose
S J Parsons
M G Caron
R J Lefkowitz
Howard Hughes Medical Institute · US

Funding

Molecular Regulation of Cardiovascular 7 TM ReceptorsR01HL016037 · NHLBI · DUKE UNIVERSITY · PI ROBERT J LEFKOWITZ · 1985 to 2026
$14.5M
REGULATION OF CYCLIC NUCLEOTIDE METABOLISMR01GM034497 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GILMAN, ALFRED G · 1985 to 2007
$5.8M
REGULATION OF CYCLIC NUCLEOTIDE METABOLISMR37GM034497 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI GILMAN, ALFRED G · 1990 to 1998
–
MOLECULAR PROPERTIES OF CARDIAC ADRENERGIC RECEPTORSR37HL016037 · NHLBI · DUKE UNIVERSITY · PI LEFKOWITZ, ROBERT J · 1986 to 1995
–
NHLBI NIH HHS HL16037NIGMS NIH HHS GM34497
6 · The paper itself

Abstract

A number of lines of evidence suggest that cross-talk exists between the cellular signal transduction pathways involving tyrosine phosphorylation catalyzed by members of the pp60c-src kinase family and those mediated by guanine nucleotide regulatory proteins (G proteins). In this study, we explore the possibility that direct interactions between pp60c-src and G proteins may occur with functional consequences. Preparations of pp60c-src isolated by immunoprecipitation phosphorylate on tyrosine residues the purified G-protein alpha subunits (G alpha) of several heterotrimeric G proteins. Phosphorylation is highly dependent on G-protein conformation, and G alpha(GDP) uncomplexed by beta gamma subunits appears to be the preferred substrate. In functional studies, phosphorylation of stimulatory G alpha (G alpha s) modestly increases the rate of binding of guanosine 5'-[gamma-[35S]thio]triphosphate to Gs as well as the receptor-stimulated steady-state rate of GTP hydrolysis by Gs. Heterotrimeric G proteins may represent a previously unappreciated class of potential substrates for pp60c-src.

Indexed as

AnimalsFluoridesGTP-Binding ProteinsGuanine NucleotidesGuanosine 5'-O-(3-Thiotriphosphate)PhosphoproteinsPhosphorylationPhosphotyrosineProtein ConformationProto-Oncogene Proteins pp60(c-src)Signal TransductionStructure-Activity RelationshipTyrosineFluoridesGTP-Binding ProteinsGuanine NucleotidesGuanosine 5'-O-(3-Thiotriphosphate)PhosphoproteinsPhosphotyrosineProto-Oncogene Proteins pp60(c-src)Tyrosine

Identifiers

PMID1378615
PMCPMC49368
OpenAlexW2066810533

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.