Evidence map›Paper›PMID 16135826›Full record

ArticleMolecular and cellular biology2005

The phosducin-like protein PhLP1 is essential for G{beta}{gamma} dimer formation in Dictyostelium discoideum.

Jaco C Knol, Ruchira Engel, Mieke Blaauw, Antonie J W G Visser, Peter J M van Haastert

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

22 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Function and Regulation of Heterotrimeric G Proteins during Chemotaxis.International journal of molecular sciences · 2016
    Review
  5. Review
  6. Article
  7. Article
  8. Phosducin-like protein 1 is essential for G-protein assembly and signaling in retinal rod photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  9. Article
  10. G protein trafficking.Sub-cellular biochemistry · 2012
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

5 authors at 1 institution in 1 country.

Jaco C KnolDepartment of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Ruchira Engel
Mieke Blaauw
Antonie J W G Visser
Peter J M van Haastert
University of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosducin proteins are known to inhibit G protein-mediated signaling by sequestering Gbetagamma subunits. However, Dictyostelium discoideum cells lacking the phosducin-like protein PhLP1 display defective rather than enhanced G protein signaling. Here we show that green fluorescent protein (GFP)-tagged Gbeta (GFP-Gbeta) and GFP-Ggamma subunits exhibit drastically reduced steady-state levels and are absent from the plasma membrane in phlp1(-) cells. Triton X-114 partitioning suggests that lipid attachment to GFP-Ggamma occurs in wild-type cells but not in phlp1(-) and gbeta(-) cells. Moreover, Gbetagamma dimers could not be detected in vitro in coimmunoprecipitation assays with phlp1(-) cell lysates. Accordingly, in vivo diffusion measurements using fluorescence correlation spectroscopy showed that while GFP-Ggamma proteins are present in a complex in wild-type cells, they are free in phlp1(-) and gbeta(-) cells. Collectively, our data strongly suggest the absence of Gbetagamma dimer formation in Dictyostelium cells lacking PhLP1. We propose that PhLP1 serves as a cochaperone assisting the assembly of Gbeta and Ggamma into a functional Gbetagamma complex. Thus, phosducin family proteins may fulfill hitherto unsuspected biosynthetic functions.

Indexed as

AnimalsCell MembraneCytosolDictyosteliumDimerizationGreen Fluorescent ProteinsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsImmunoprecipitationMolecular ChaperonesNerve Tissue ProteinsOctoxynolPolyethylene GlycolsProtein SubunitsG-protein Beta gammaGreen Fluorescent ProteinsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsMolecular ChaperonesNerve Tissue ProteinsNonidet P-40OctoxynolPolyethylene GlycolsProtein Subunits

Identifiers

PMID16135826
PMCPMC1234308
OpenAlexW2164531655

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.