Evidence map›Paper›PMID 17658730›Full record

ReviewCellular signalling2007

Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding.

Barry M Willardson, Alyson C Howlett

Open access · greenAbstract readReview
In one paragraph

Review in Cellular signalling, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

64 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Challenges and Opportunities Arising from Host-International journal of molecular sciences · 2024
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Phosducin-like proteinFrontiers in microbiology · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Snapshots of actin and tubulin folding inside the TRiC chaperonin.Nature structural & molecular biology · 2022
    Article
  17. Frontiers in molecular biosciences · 2022
    Article
  18. Article
  19. Article
  20. Review

4 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Barry M WillardsonDepartment of Chemistry and Biochemistry, C-100 BNSN, Brigham Young University Provo, Utah 84602, USA. bmwillardson@chem.byu.edu
Alyson C Howlett
Brigham Young University · US

Funding

Structural basis for chaperone-dependent folding of beta-propeller proteins essential for visionR01EY012287 · NEI · BRIGHAM YOUNG UNIVERSITY · PI WILLARDSON, BARRY M · 1999 to 2022
$5.7M
Co-chaperone role of phosducin-like protein in G protein subunit assemblyR01GM078550 · NIGMS · BRIGHAM YOUNG UNIVERSITY · PI WILLARDSON, BARRY M · 2007 to 2010
$1.3M
NEI NIH HHS EY12278NEI NIH HHS R01 EY012287NIGMS NIH HHS R01 GM078550
6 · The paper itself

Abstract

Members of the phosducin gene family were initially proposed to act as down-regulators of G protein signaling by binding G protein betagamma dimers (Gbetagamma) and inhibiting their ability to interact with G protein alpha subunits (Galpha) and effectors. However, recent findings have over-turned this hypothesis by showing that most members of the phosducin family act as co-chaperones with the cytosolic chaperonin complex (CCT) to assist in the folding of a variety of proteins from their nascent polypeptides. In fact rather than inhibiting G protein pathways, phosducin-like protein 1 (PhLP1) has been shown to be essential for G protein signaling by catalyzing the folding and assembly of the Gbetagamma dimer. PhLP2 and PhLP3 have no role in G protein signaling, but they appear to assist in the folding of proteins essential in regulating cell cycle progression as well as actin and tubulin. Phosducin itself is the only family member that does not participate with CCT in protein folding, but it is believed to have a specific role in visual signal transduction to chaperone Gbetagamma subunits as they translocate to and from the outer and inner segments of photoreceptor cells during light-adaptation.

Indexed as

Protein FoldingSignal TransductionActinsAmino Acid SequenceAnimalsCarrier ProteinsCell Cycle ProteinsChaperonin Containing TCP-1ChaperoninsEye ProteinsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsGTP-Binding Protein RegulatorsHumansModels, MolecularMolecular ChaperonesActinsCarrier ProteinsCell Cycle ProteinsChaperonin Containing TCP-1ChaperoninsEye ProteinsG-protein Beta gammaGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsGTP-Binding Protein RegulatorsMolecular ChaperonesNerve Tissue ProteinsPDCL2 protein, humanPDCL3 protein, humanPDCL protein, humanphosducinPhosphoproteinsTubulin

Identifiers

PMID17658730
PMCPMC2095786
OpenAlexW2078094267

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.