Evidence map›Paper›PMID 1409685›Full record

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

Myristoylation of the G alpha i2 polypeptide, a G protein alpha subunit, is required for its signaling and transformation functions.

C Gallego, S K Gupta, S Winitz, B J Eisfelder, G L Johnson

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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 10% 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, 45 citations in OpenAlex.

  1. Review
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  8. Review
  9. Mapping the interface between calmodulin and MARCKS-related protein by fluorescence spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
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  14. Pheromone action regulates G-protein alpha-subunit myristoylation in the yeast Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 1993
    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 2 institutions in 1 country.

C GallegoDivision of Basic Sciences, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.
S K Gupta
S Winitz
B J Eisfelder
G L Johnson
National Jewish Health · USUniversity of Colorado Denver · US

Funding

RECEPTOR INTERACTION WITH GTP REGULATORY PROTEINSR37GM030324 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JOHNSON, GARY L. · 1999 to 2008
$3.7M
REGULATION OF SEQUENTIAL PROTEIN KINASE PATHWAYSR01DK037871 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JOHNSON, GARY L. · 1986 to 2011
$3.7M
REGULATORY PROTEINS OF ADENYLATE CYCLASER01GM030324 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JOHNSON, GARY L. · 1985 to 2012
$1.8M
NIDDK NIH HHS DK37871NIGMS NIH HHS GM30324
6 · The paper itself

Abstract

GTPase-inhibiting mutations of the alpha subunit (alpha i2) of the G protein, Gi2, result in constitutive activation of alpha i2 signal transduction functions. GTPase-inhibited alpha i2 mutant polypeptides, referred to as gip2 oncoproteins, have glutamine-205 mutated to leucine (alpha i2Q205L). Expression of the alpha i2Q205L polypeptide inhibits adenylyl cyclase stimulation, constitutively activates p42 mitogen-activated protein kinase, and transforms Rat 1a fibroblasts. The alpha i2 polypeptides are N-terminal-myristoylated, but the function of myristoylation is unclear in alpha i2 signal transduction. We have tested the requirement for myristoylation on the ability of the alpha i2Q205L mutant polypeptide to constitutively regulate signal pathways and cell transformation. When expressed in Rat 1a cells, the nonmyristoylated alpha i2Q205L polypeptide is membrane associated but is unable to regulate adenylyl cyclase or p42 mitogen-activated protein kinase and does not induce cellular transformation. We conclude that myristoylation is absolutely necessary for alpha i2Q205L signal transduction and regulation of effector enzymes in the cell.

Indexed as

Adenylate Cyclase ToxinAnimalsCell Transformation, NeoplasticChlorocebus aethiopsGTP-Binding ProteinsGTP PhosphohydrolasesIn Vitro TechniquesMyristatesProtein KinasesProtein Processing, Post-TranslationalRatsSignal TransductionStructure-Activity RelationshipTransfectionVirulence Factors, BordetellaAdenylate Cyclase ToxinGTP-Binding ProteinsGTP PhosphohydrolasesMyristatesProtein KinasesVirulence Factors, Bordetella

Identifiers

PMID1409685
PMCPMC50199
OpenAlexW2008286131

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.