Evidence map›Paper›PMID 10523659›Full record

ArticleMolecular and cellular biology1999

Dual lipid modification of the yeast ggamma subunit Ste18p determines membrane localization of Gbetagamma.

J E Hirschman, D D Jenness

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Regulation of large and small G proteins by ubiquitination.The Journal of biological chemistry · 2019
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Chemical gradients and chemotropism in yeast.Cold Spring Harbor perspectives in biology · 2009
    Review
  16. Article
  17. Article
  18. Article
  19. Mapping dynamic protein interactions in MAP kinase signaling using live-cell fluorescence fluctuation spectroscopy and imaging.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  20. 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.

J E HirschmanDepartment of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655-0122, USA.
D D Jenness
University of Massachusetts Chan Medical School · US

Funding

CONTROL OF ALPHA FACTOR RECEPTOR ACTIVITY IN YEAST CELLSR01GM034719 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JENNESS, DUANE D · 1985 to 2004
$1.6M
NIGMS NIH HHS GM34719NIGMS NIH HHS R01 GM034719
6 · The paper itself

Abstract

The pheromone response in the yeast Saccharomyces cerevisiae is mediated by a heterotrimeric G protein. The Gbetagamma subunit (a complex of Ste4p and Ste18p) is associated with both internal and plasma membranes, and a portion is not stably associated with either membrane fraction. Like Ras, Ste18p contains a farnesyl-directing CaaX box motif (C-terminal residues 107 to 110) and a cysteine residue (Cys 106) that is a potential site for palmitoylation. Mutant Ste18p containing serine at position 106 (mutation ste18-C106S) migrated more rapidly than wild-type Ste18p during sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The electrophoretic mobility of wild-type Ste18p (but not the mutant Ste18p) was sensitive to hydroxylamine treatment, consistent with palmitoyl modification at Cys 106. Furthermore, immunoprecipitation of the Gbetagamma complex from cells cultured in the presence of [(3)H]palmitic acid resulted in two radioactive species on nonreducing SDS-PAGE gels, with molecular weights corresponding to Ggamma and Gbetagamma. Substitution of serine for either Cys 107 or Cys 106 resulted in the failure of Gbetagamma to associate with membranes. The Cys 107 substitution also resulted in reduced steady-state accumulation of Ste18p, suggesting that the stability of Ste18p requires modification at Cys 107. All of the mutant forms of Ste18p formed complexes with Ste4p, as assessed by coimmunoprecipitation. We conclude that tight membrane attachment of the wild-type Gbetagamma depends on palmitoylation at Cys 106 and prenylation at Cys 107 of Ste18p.

Indexed as

Cell CompartmentationGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsProtein Processing, Post-TranslationalSaccharomyces cerevisiae ProteinsFatty Acids, UnsaturatedHeterotrimeric GTP-Binding ProteinsMembrane ProteinsMutationPalmitic AcidPalmitic AcidsProtein PrenylationSaccharomyces cerevisiaeSubstrate Specificityfarnesoic acidFatty Acids, UnsaturatedGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsHeterotrimeric GTP-Binding ProteinsMembrane ProteinsPalmitic AcidPalmitic AcidsSaccharomyces cerevisiae ProteinsSTE18 protein, S cerevisiaeSte4 protein, S cerevisiae

Identifiers

PMID10523659
PMCPMC84814
OpenAlexW2123272310

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.