Evidence map›Paper›PMID 1534749›Full record

ArticleThe EMBO journal1992

Palmitoylation alters protein activity: blockade of G(o) stimulation by GAP-43.

Y Sudo, D Valenzuela, A G Beck-Sickinger, M C Fishman, S M Strittmatter

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

30 citing papers in PubMed, 111 citations in OpenAlex.

  1. Review
  2. Review
  3. Analysis of IFITM-IFITM Interactions by a Flow Cytometry-Based FRET Assay.International journal of molecular sciences · 2019
    Article
  4. Molecular basis of the functions of the mammalian neuronal growth cone revealed using new methods.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Use of micellar electrokinetic chromatography to measure palmitoylation of a peptide.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2008
    Article
  11. Article
  12. Article
  13. Autopalmitoylation of tubulin.Protein science : a publication of the Protein Society · 2000
    Article
  14. Article
  15. Plasma membrane localization is required for RGS4 function in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  16. Article
  17. Article
  18. GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  19. 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

5 authors at 1 institution in 1 country.

Y SudoDevelopmental Biology Laboratory, Massachusetts General Hospital, Charlestown.
D Valenzuela
A G Beck-Sickinger
M C Fishman
S M Strittmatter
Massachusetts General Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The addition of palmitate to cysteine residues enhances the hydrophobicity of proteins, and consequently their membrane association. Here we have investigated whether this type of fatty acylation also regulates protein-protein interactions. GAP-43 is a neuronal protein that increases guanine nucleotide exchange by heterotrimeric G proteins. Two cysteine residues near the N-terminus of GAP-43 are subject to palmitoylation, and are necessary for membrane binding as well as for G(o) activation. N-terminal peptides, which include these cysteines, stimulate G(o). Monopalmitoylation reduces, and dipalmitoylation abolishes the activity of the peptides. The activity of GAP-43 protein purified from brain also is reversibly blocked by palmitoylation. This suggests that palmitoylation controls a cycle of GAP-43 between an acylated, membrane-bound reservoir of inactive GAP-43, and a depalmitoylated, active pool of protein.

Indexed as

AnimalsBrainCattleGAP-43 ProteinGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)KineticsMembrane GlycoproteinsNerve Tissue ProteinsPalmitic AcidPalmitic AcidsPeptide FragmentsPhosphoproteinsProtein BindingGAP-43 ProteinGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Membrane GlycoproteinsNerve Tissue ProteinsPalmitic AcidPalmitic AcidsPeptide FragmentsPhosphoproteins

Identifiers

PMID1534749
PMCPMC556676
OpenAlexW136758419

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.