Evidence map›Paper›PMID 17360629›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Regulation of brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) and BIG2 activity via PKA and protein phosphatase 1gamma.

Fuminobu Kuroda, Joel Moss, Martha Vaughan

Open access · greenAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

29 citing papers in PubMed, 47 citations in OpenAlex.

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  8. Article
  9. Enhancement of β-catenin activity by BIG1 plus BIG2 via Arf activation and cAMP signals.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Unfolded protein response regulates yeast small GTPase Arl1p activation at late Golgi via phosphorylation of Arf GEF Syt1p.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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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

3 authors at 2 institutions in 1 country.

Fuminobu KurodaPulmonary-Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892-1434, USA.
Joel Moss
Martha Vaughan
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Molecular Characterization and Regulation of GTP-binding ProteinsZIAHL000627 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI VAUGHAN, MARTHA · 2009 to 2016
$8.4M
REGULATION OF GTP-BINDING PROTEINSZ01HL000627 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI VAUGHAN, MARTHA · 1985 to 2008
$4.5M
Intramural NIH HHS
6 · The paper itself

Abstract

Brefeldin A-inhibited guanine nucleotide-exchange proteins (GEPs) BIG1 and BIG2 activate ADP-ribosylation factor (ARF) GTPases, which are required for vesicular trafficking. Both molecules contain one or more sites for binding protein kinase A, i.e., A kinase-anchoring protein (AKAP) sequences. Elevation of cell cAMP caused PKA-catalyzed phosphorylation and nuclear accumulation of BIG1 but not BIG2. We then asked whether BIG1 phosphorylation altered its GEP activity. Incubation of BIG1 or BIG2 with PKA catalytic subunits and ATP resulted in retardation of their electrophoretic migration, consistent with PKA phosphorylation. Okadaic acid inhibits many protein phosphatases, including protein phosphatase 1 (PP1) and PP2A, that can reverse PKA-catalyzed phosphorylation. Incubation of HepG2 cells with okadaic acid caused concentration-dependent accumulation of presumably phosphorylated BIG1 and BIG2 with decreased mobility, which was increased by subsequent incubation in vitro with specific recombinant phosphatases, PP1gamma > PP2A >> PP1alpha. For assays of GEP activity, BIG1 and BIG2 were immunoprecipitated from cells that had been depleted, respectively, of BIG2 and BIG1 by using specific siRNA. GEP activity of each was significantly decreased after incubation with recombinant PKA plus ATP and restored by incubation with PP1gamma. In agreement with a role for PP1gamma in regulation of BIG, endogenous PP1gamma, but not PP1alpha or beta, was immunoprecipitated with BIG1 or BIG2 from microsomal fractions. All observations are consistent with the effects of BIG1 and BIG2 phosphorylation on vesicular trafficking, via alterations in ARF activation and regulatory roles for cAMP, PKA, and PP1gamma in ARF activation by BIG1 and BIG2.

Indexed as

Adenosine TriphosphateADP-Ribosylation FactorsBlotting, WesternCell Line, TumorCyclic AMP-Dependent Protein KinasesGuanine Nucleotide Exchange FactorsHumansImmunoprecipitationMicroscopy, FluorescenceOkadaic AcidPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Vesicular Transport ProteinsAdenosine TriphosphateADP-Ribosylation FactorsARFGEF1 protein, humanCyclic AMP-Dependent Protein KinasesGuanine Nucleotide Exchange FactorsOkadaic AcidPhosphoprotein PhosphatasesProtein Phosphatase 1Vesicular Transport Proteins

Identifiers

PMID17360629
PMCPMC1805514
OpenAlexW1986882870

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.