Evidence map›Paper›PMID 7980434›Full record

ArticleThe Biochemical journal1994

N-terminal fatty acylation of the alpha-subunit of the G-protein Gi1: only the myristoylated protein is a substrate for palmitoylation.

F Galbiati, F Guzzi, A I Magee, G Milligan, M Parenti

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1994. 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
1.8field-weighted citation impact, top 15% 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, 50 citations in OpenAlex.

  1. Article
  2. The polybasic puzzle: how N-terminal charges modulate GαiCell communication and signaling : CCS · 2025
    Article
  3. Amino acid and protein specificity of protein fatty acylation inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Genome-Wide Identification and Characterization ofInternational journal of molecular sciences · 2021
    Article
  7. Article
  8. Review
  9. Article
  10. G protein trafficking.Sub-cellular biochemistry · 2012
    Review
  11. G-protein signaling: back to the future.Cellular and molecular life sciences : CMLS · 2005
    Review
  12. Article
  13. Review
  14. Article
  15. 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

5 authors at 1 institution in 1 country.

F GalbiatiDipartimento di Farmacologia, Università di Milano, Italy.
F Guzzi
A I Magee
G Milligan
M Parenti
University of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The alpha-subunit of the G-protein Gi1 carries two fatty acyl moieties covalently bound to its N-terminal region: myristic acid is linked to glycine-2 and palmitic acid is linked to cysteine-3. Using site-directed mutagenesis on a cDNA construct of alpha i1 we have generated an alpha i1-G2A mutant, carrying alanine instead of glycine at position 2, and alpha i1-C3S mutant, in which serine replaced cysteine-3 and a double mutant with both substitutions (alpha i1-G2A/C3S). These constructs were individually expressed by transfection in Cos-7 cells, and incorporation of fatty acids into the various mutants was compared with wild-type alpha i1 monitoring metabolic labelling with [3H]palmitate or [3H]myristate. The disruption of the palmitoylation site in alpha i1-C3S did not influence myristoylation, whereas prevention of myristoylation in alpha i1-G2A also abolished palmitoylation. Co-translational myristoylation is thus an absolute requirement for alpha i1 to be post-translationally palmitoylated. The non-palmitoylated alpha i1-C3S showed reduced membrane binding to the same extent as the non-myristoylated/non-palmitoylated alpha i1-G2A and alpha i1-G2A/C3S mutants, indicating that the attachment of palmitic acid is necessary for proper interaction with the membrane.

Indexed as

AcylationAnimalsBase SequenceBinding SitesCell LineDNA, ComplementaryFatty AcidsGTP-Binding ProteinsMolecular Sequence DataMutagenesis, Site-DirectedMyristic AcidMyristic AcidsPalmitic AcidPalmitic AcidsRatsDNA, ComplementaryFatty AcidsGTP-Binding ProteinsMyristic AcidMyristic AcidsPalmitic AcidPalmitic Acids

Identifiers

PMID7980434
PMCPMC1137601
OpenAlexW80630166

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.