Evidence map›Paper›PMID 26160508›Full record

ArticleMethods (San Diego, Calif.)2016

Exploring G protein-coupled receptor signaling networks using SILAC-based phosphoproteomics.

Grace R Williams, Jennifer R Bethard, Mary N Berkaw, Alexis K Nagel, Louis M Luttrell, Lauren E Ball

Open access · greenAbstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. 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.

Grace R WilliamsDepartment of Molecular and Cellular Pharmacology, Medical University of South Carolina, Charleston, SC 29425, USA.
Jennifer R BethardDepartment of Molecular and Cellular Pharmacology, Medical University of South Carolina, Charleston, SC 29425, USA.
Mary N BerkawDepartment of Molecular and Cellular Pharmacology, Medical University of South Carolina, Charleston, SC 29425, USA.
Alexis K NagelDepartment of Molecular and Cellular Pharmacology, Medical University of South Carolina, Charleston, SC 29425, USA; Department of Oral Health Sciences, Medical University of South Carolina, Charleston, SC 29425, USA.
Louis M LuttrellDepartment of Medicine, Medical University of South Carolina, Charleston, SC 29425, USA; Research Service of the Ralph H. Johnson Veterans Affairs Medical Center, Charleston, SC 29401, USA.
Lauren E BallDepartment of Molecular and Cellular Pharmacology, Medical University of South Carolina, Charleston, SC 29425, USA; Department of Oral Health Sciences, Medical University of South Carolina, Charleston, SC 29425, USA. Electronic address: ballle@musc.edu.
Medical University of South Carolina · USRalph H. Johnson VA Medical Center · US

Funding

SOUTH CAROLINA COBRE IN OXIDANTS, REDOX BALANCE AND STRESS SIGNALINGP20GM103542 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI TEW, KENNETH D. · 2012 to 2020
$20.2M
TYROSINE KINASES IN G PROTEIN MEDIATED SIGNALINGR01DK055524 · NIDDK · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI LUTTRELL, LOUIS M · 1998 to 2017
$4.6M
Regulation of IGF-1 and Insulin Signaling by O-GlcNAc GlycosylationR01DE020925 · NIDCR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI BALL, LAUREN ELIZABETH · 2010 to 2014
$1.8M
Pharmacodynamics of Biased G protein-Coupled Receptor AgonismR01GM095497 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI LUTTRELL, LOUIS M · 2013 to 2016
$1.1M
Orbitrap Mass SpectrometerS10OD010731 · OD · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI BALL, LAUREN ELIZABETH · 2012 to 2012
$600k
NIDCR NIH HHS R01 DE020925NIDDK NIH HHS R01 DK055524NIGMS NIH HHS P20 GM103542NIGMS NIH HHS R01 GM095497NIH HHS S10 OD010731PHS HHS S10 D010731
6 · The paper itself

Abstract

The type 1 parathyroid hormone receptor (PTH1R) is a key regulator of calcium homeostasis and bone turnover. Here, we employed SILAC-based quantitative mass spectrometry and bioinformatic pathways analysis to examine global changes in protein phosphorylation following short-term stimulation of endogenously expressed PTH1R in osteoblastic cells in vitro. Following 5min exposure to the conventional agonist, PTH(1-34), we detected significant changes in the phosphorylation of 224 distinct proteins. Kinase substrate motif enrichment demonstrated that consensus motifs for PKA and CAMK2 were the most heavily upregulated within the phosphoproteome, while consensus motifs for mitogen-activated protein kinases were strongly downregulated. Signaling pathways analysis identified ERK1/2 and AKT as important nodal kinases in the downstream network and revealed strong regulation of small GTPases involved in cytoskeletal rearrangement, cell motility, and focal adhesion complex signaling. Our data illustrate the utility of quantitative mass spectrometry in measuring dynamic changes in protein phosphorylation following GPCR activation.

Indexed as

ProteomicsAnimalsCell Line, TransformedGene Regulatory NetworksMiceParathyroid HormoneReceptor, Parathyroid Hormone, Type 1Receptors, G-Protein-CoupledSignal TransductionTandem Mass SpectrometryParathyroid HormonePTH1R protein, humanReceptor, Parathyroid Hormone, Type 1Receptors, G-Protein-CoupledG protein-coupled receptorMass spectrometryOsteoblastParathyroid hormone receptorPhosphoproteomics

Identifiers

PMID26160508
PMCPMC4696908
OpenAlexW846458259

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.