Evidence map›Paper›PMID 20852191›Full record

ArticleMolecular & cellular proteomics : MCP2011

Disruption of the chaperonin containing TCP-1 function affects protein networks essential for rod outer segment morphogenesis and survival.

Ekaterina Posokhova, Hongman Song, Marycharmain Belcastro, LeeAnn Higgins, Lauren R Bigley, Norman A Michaud, Kirill A Martemyanov, Maxim Sokolov

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Essential role of the chaperonin CCT in rod outer segment biogenesis.Investigative ophthalmology & visual science · 2014
    Article
  16. Article
  17. Article
  18. Article
  19. 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
  20. 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

8 authors at 3 institutions in 1 country.

Ekaterina PosokhovaDepartment of Pharmacology, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Hongman Song
Marycharmain Belcastro
LeeAnn Higgins
Lauren R Bigley
Norman A Michaud
Kirill A Martemyanov
Maxim Sokolov
University of Minnesota · USWest Virginia University · USMassachusetts Eye and Ear Infirmary · US

Funding

Regulation of Signaling in the Retina by RGS ProteinsR01EY018139 · NEI · UNIVERSITY OF MINNESOTA · PI MARTEMYANOV, KIRILL A. · 2007 to 2025
$8.9M
Assembly and Trafficking of Heterotrimeric G Proteins in Vertebrate PhotoreceptorR01EY019665 · NEI · WEST VIRGINIA UNIVERSITY · PI SOKOLOV, MAXIM · 2009 to 2013
$1.6M
Molecular Basis of RGS Protein Function in the StriatumK02DA026405 · NIDA · UNIVERSITY OF MINNESOTA · PI MARTEMYANOV, KIRILL A. · 2009 to 2019
$1.2M
NEI NIH HHS EY018139NEI NIH HHS EY019665NEI NIH HHS R01 EY018139NEI NIH HHS R01 EY019665NIDA NIH HHS DA026405NIDA NIH HHS K02 DA026405
6 · The paper itself

Abstract

Type II Chaperonin Containing TCP-1 (CCT, also known as TCP-1 Ring Complex, TRiC) is a multi-subunit molecular machine thought to assist in the folding of ∼ 10% of newly translated cytosolic proteins in eukaryotes. A number of proteins folded by CCT have been identified in yeast and cultured mammalian cells, however, the function of this chaperonin in vivo has never been addressed. Here we demonstrate that suppressing the CCT activity in mouse photoreceptors by transgenic expression of a dominant-negative mutant of the CCT cofactor, phosducin-like protein (PhLP), results in the malformation of the outer segment, a cellular compartment responsible for light detection, and triggers rapid retinal degeneration. Investigation of the underlying causes by quantitative proteomics identified distinct protein networks, encompassing ∼ 200 proteins, which were significantly affected by the chaperonin deficiency. Notably among those were several essential proteins crucially engaged in structural support and visual signaling of the outer segment such as peripherin 2, Rom1, rhodopsin, transducin, and PDE6. These data for the first time demonstrate that normal CCT function is ultimately required for the morphogenesis and survival of sensory neurons of the retina, and suggest the chaperonin CCT deficiency as a potential, yet unexplored, cause of neurodegenerative diseases.

Indexed as

MorphogenesisAmino Acid SequenceAnimalsCarrier ProteinsCell SurvivalChaperonin Containing TCP-1Down-RegulationLight Signal TransductionMiceMice, TransgenicMolecular ChaperonesMolecular Sequence DataMutant ProteinsNerve Tissue ProteinsProteomeRod Cell Outer SegmentCarrier ProteinsChaperonin Containing TCP-1Molecular ChaperonesMutant ProteinsNerve Tissue ProteinsPdcl protein, mouseProteome

Identifiers

PMID20852191
PMCPMC3013443
OpenAlexW2128525434

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.