Evidence map›Paper›PMID 22329346›Full record

ArticleBiochemistry2012

Myristoylation exerts direct and allosteric effects on Gα conformation and dynamics in solution.

Anita M Preininger, Ali I Kaya, James A Gilbert, Laura S Busenlehner, Richard N Armstrong, Heidi E Hamm

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Protein sorting, targeting and trafficking in photoreceptor cells.Progress in retinal and eye research · 2013
    Review
  11. Review
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

6 authors at 2 institutions in 1 country.

Anita M PreiningerVanderbilt University Medical Center, Nashville, Tennessee 37232, United States.
Ali I Kaya
James A Gilbert
Laura S Busenlehner
Richard N Armstrong
Heidi E Hamm
Vanderbilt University Medical Center · USUniversity of Alabama · US

Funding

VANDERBILT UNIVERSITY CTSA FOR PEDIATRIC RESEARCHUL1RR024975 · NCRR · VANDERBILT UNIVERSITY · PI BERNARD, GORDON RAPHAEL · 2007 to 2011
$45.7M
IMMUNOLOGICAL STUDIES OF VISUAL TRANSDUCTION PATHWAYSR01EY006062 · NEI · VANDERBILT UNIVERSITY · PI HAMM, HEIDI E · 1985 to 2017
$5.6M
MECHANISM OF ACTION OF GLUTATHIONE S-TRANSFERASER01GM030910 · NIGMS · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R · 1985 to 2016
$4.7M
The Vanderbilt Institute for Clinical and Translational Research (VICTR) KL2KL2RR024977 · NCRR · VANDERBILT UNIVERSITY · PI BERNARD, GORDON RAPHAEL · 2007 to 2011
$3.0M
The Vanderbilt Institute for Clinical and Translational Research (VICTR) TL1TL1RR024978 · NCRR · VANDERBILT UNIVERSITY · PI BERNARD, GORDON RAPHAEL · 2007 to 2011
$1.3M
NCRR NIH HHS KL2 RR024977NCRR NIH HHS TL1 RR024978NCRR NIH HHS UL1 RR024975NEI NIH HHS R01 EY006062NEI NIH HHS R01 EY06062NIGMS NIH HHS R01 GM030910
6 · The paper itself

Abstract

Coupling of heterotrimeric G proteins to activated G protein-coupled receptors results in nucleotide exchange on the Gα subunit, which in turn decreases its affinity for both Gβγ and activated receptors. N-Terminal myristoylation of Gα subunits aids in membrane localization of inactive G proteins. Despite the presence of the covalently attached myristoyl group, Gα proteins are highly soluble after GTP binding. This study investigated factors facilitating the solubility of the activated, myristoylated protein. In doing so, we also identified myristoylation-dependent differences in regions of Gα known to play important roles in interactions with receptors, effectors, and nucleotide binding. Amide hydrogen-deuterium exchange and site-directed fluorescence of activated proteins revealed a solvent-protected amino terminus that was enhanced by myristoylation. Furthermore, fluorescence quenching confirmed that the myristoylated amino terminus is in proximity to the Switch II region in the activated protein. Myristoylation also stabilized the interaction between the guanine ring and the base of the α5 helix that contacts the bound nucleotide. The allosteric effects of myristoylation on protein structure, function, and localization indicate that the myristoylated amino terminus of Gα(i) functions as a myristoyl switch, with implications for myristoylation in the stabilization of nucleotide binding and in the spatial regulation of G protein signaling.

Indexed as

Allosteric RegulationAnimalsDeuterium Exchange MeasurementGTP-Binding Protein alpha Subunits, Gi-GoModels, MolecularMyristic AcidProtein ConformationRatsSignal TransductionSolutionsGTP-Binding Protein alpha Subunits, Gi-GoMyristic AcidSolutions

Identifiers

PMID22329346
PMCPMC3312377
OpenAlexW2026633461

What OpenQuestion holds

Textmetadata
LicenceTDM
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.