Evidence map›Paper›PMID 18172023›Full record

ArticleMolecular biology of the cell2008

Dissection of the carboxyl-terminal domain of the proteasomal subunit Rpn11 in maintenance of mitochondrial structure and function.

Teresa Rinaldi, Line Hofmann, Alessia Gambadoro, Raynald Cossard, Nurit Livnat-Levanon, Michael H Glickman, Laura Frontali, Agnès Delahodde

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
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  12. Article
  13. Article
  14. Functions of the 19S complex in proteasomal degradation.Trends in biochemical sciences · 2013
    Review
  15. Article
  16. Article
  17. Near-atomic resolution structural model of the yeast 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  18. Article
  19. Article
  20. Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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 3 countries.

Teresa RinaldiPasteur Institute-Cenci Bolognetti Foundation, Department of Cell and Developmental Biology, University of Rome La Sapienza, 00185 Rome, Italy. teresa.rinaldi@uniroma1.it
Line Hofmann
Alessia Gambadoro
Raynald Cossard
Nurit Livnat-Levanon
Michael H Glickman
Laura Frontali
Agnès Delahodde
Istituto Pasteur · ITUniversité Paris-Sud · FRTechnion – Israel Institute of Technology · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously demonstrated that the C-terminal part of Rpn11, a deubiquitinating enzyme in the lid of the proteasome, is essential for maintaining a correct cell cycle and normal mitochondrial morphology and function. The two roles are apparently unlinked as the mitochondrial role is mapped to the Carboxy-terminus, whereas the catalytic deubiquitinating activity is found within the N-terminal region. The mitochondrial defects are observed in rpn11-m1 (originally termed mpr1-1), a mutation that generates Rpn11 lacking the last 31 amino acids. No mitochondrial phenotypes are recorded for mutations in the MPN+/JAMM motif. In the present study, we investigated the participation of the last 31 amino acids of the Rpn11 protein by analysis of intragenic revertants and site-specific mutants. We identified a putative alpha-helix necessary for the maintenance of a correct cell cycle and determined that a very short region at the C-terminus of Rpn11 is essential for the maintenance of tubular mitochondrial morphology. Furthermore, we show that expression of the C-terminal part of Rpn11 is able to complement in trans all of the rpn11-m1 mitochondrial phenotypes. Finally, we investigate the mechanisms by which Rpn11 controls the mitochondrial shape and show that Rpn11 may regulate the mitochondrial fission and tubulation processes.

Indexed as

Amino Acid SequenceEndopeptidasesGreen Fluorescent ProteinsMitochondriaMolecular Sequence DataMutagenesis, Site-DirectedOxygen ConsumptionPhenotypeProteasome Endopeptidase ComplexProtein BindingProtein Structure, TertiaryProtein SubunitsProtein TransportRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEndopeptidasesGreen Fluorescent ProteinsProteasome Endopeptidase ComplexProtein SubunitsRecombinant Fusion ProteinsRPN11 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID18172023
PMCPMC2262987
OpenAlexW2019179677

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.