Evidence map›Paper›PMID 18566450›Full record

ArticleThe Journal of biological chemistry2008

The PDZ and band 4.1 containing protein Frmpd1 regulates the subcellular location of activator of G-protein signaling 3 and its interaction with G-proteins.

Ningfei An, Joe B Blumer, Michael L Bernard, Stephen M Lanier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

27 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. AGS-3 alters Caenorhabditis elegans behavior after food deprivation via RIC-8 activation of the neural G protein G αo.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    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

4 authors at 1 institution in 1 country.

Ningfei AnDepartment of Pharmacology and Experimental Therapeutics, Louisiana State University Health Sciences Center, New Orleans, Louisiana 70112, USA.
Joe B Blumer
Michael L Bernard
Stephen M Lanier
Medical University of South Carolina · US

Funding

STRUCTURAL ANALYSIS OF THE ALPHA-2 ADRENERGIC RECEPTORR01NS024821 · NINDS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI LANIER, STEPHEN M. · 1994 to 2007
$2.4M
Defining the role of AGS3 in G protein signal processingF32MH065092 · NIMH · LOUISIANA STATE UNIV HSC NEW ORLEANS · PI BLUMER, JOE B · 2002 to 2004
$134k
STRUCTURAL ANALYSIS OF THE ALPHA2-ADRENERGIC RECEPTORR29NS024821 · NINDS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI LANIER, STEPHEN M. · 1987 to 1991
–
NIMH NIH HHS F32 MH065092NIMH NIH HHS F32MH65092NIMH NIH HHS MH90531NINDS NIH HHS NS24821
6 · The paper itself

Abstract

Activator of G-protein signaling 3 (AGS3) is one of nine mammalian proteins containing one or more G-protein regulatory (GPR) motifs that stabilize the GDP-bound conformation of Galphai. Such proteins have revealed unexpected functional diversity for the "G-switch" in the control of events within the cell independent of the role of heterotrimeric G-proteins as transducers for G-protein-coupled receptors at the cell surface. A key question regarding this class of proteins is what controls their subcellular positioning and interaction with G-proteins. We conducted a series of yeast two-hybrid screens to identify proteins interacting with the tetratricopeptide repeat (TPR) of AGS3, which plays an important role in subcellular positioning of the protein. We report the identification of Frmpd1 (FERM and PDZ domain containing 1) as a regulatory binding partner of AGS3. Frmpd1 binds to the TPR domain of AGS3 and coimmunoprecipitates with AGS3 from cell lysates. Cell fractionation indicated that Frmpd1 stabilizes AGS3 in a membrane fraction. Upon cotransfection of COS7 cells with Frmpd1-GFP and AGS3-mRFP, AGS3-mRFP is observed in regions of the cell cortex and also in membrane extensions or processes where it appears to be colocalized with Frmpd1-GFP based upon the merged fluorescent signals. Frmpd1 knockdown (siRNA) in Cath.a-differentiated neuronal cells decreased the level of endogenous AGS3 in membrane fractions by approximately 50% and enhanced the alpha2-adrenergic receptor-mediated inhibition of forskolin-induced increases in cAMP. The coimmunoprecipitation of Frmpd1 with AGS3 is lost as the amount of Galphai3 in the cell is increased and AGS3 apparently switches its binding partner from Frmpd1 to Galphai3 indicating that the interaction of AGS3 with Frmpd1 and Galphai3 is mutually exclusive. Mechanistically, Frmpd1 may position AGS3 in a membrane environment where it then interacts with Galphai in a regulated manner.

Indexed as

Amino Acid MotifsAnimalsCarrier ProteinsCell MembraneChlorocebus aethiopsColforsinCOS CellsCytoskeletal ProteinsGTP-Binding Protein alpha SubunitsGuanine Nucleotide Dissociation InhibitorsHumansMembrane ProteinsPDZ DomainsProtein TransportRatsReceptors, Adrenergic, alpha-2Carrier ProteinsColforsinCytoskeletal Proteinserythrocyte membrane band 4.1 proteinFrmpd1 protein, humanFrmpd1 protein, ratGPSM1 protein, humanGpsm1 protein, ratGTP-Binding Protein alpha SubunitsGuanine Nucleotide Dissociation InhibitorsMembrane ProteinsReceptors, Adrenergic, alpha-2RNA, Small Interfering

Identifiers

PMID18566450
PMCPMC2529004
OpenAlexW1982442831

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.