Evidence map›Paper›PMID 10366593›Full record

ArticleThe Journal of cell biology1999

A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae.

H A Fisk, M P Yaffe

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
3.9field-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

77 citing papers in PubMed, 178 citations in OpenAlex.

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  14. ThreeFrontiers in plant science · 2016
    Article
  15. Review
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  20. Review

17 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.

H A FiskUniversity of California, San Diego, Department of Biology, La Jolla, California 92093, USA.
M P Yaffe
University of California, San Diego · US

Funding

MECHANISMS OF MITOCHONDRIAL DIVISION AND INHERITANCER01GM044614 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI YAFFE, MICHAEL P. · 1993 to 2004
$1.4M
NIGMS NIH HHS GM44614NIGMS NIH HHS R01 GM044614
6 · The paper itself

Abstract

The smm1 mutation suppresses defects in mitochondrial distribution and morphology caused by the mdm1-252 mutation in the yeast Saccharomyces cerevisiae. Cells harboring only the smm1 mutation themselves display temperature-sensitive growth and aberrant mitochondrial inheritance and morphology at the nonpermissive temperature. smm1 maps to RSP5, a gene encoding an essential ubiquitin-protein ligase. The smm1 defects are suppressed by overexpression of wild-type ubiquitin but not by overexpression of mutant ubiquitin in which lysine-63 is replaced by arginine. Furthermore, overexpression of this mutant ubiquitin perturbs mitochondrial distribution and morphology in wild-type cells. Site-directed mutagenesis revealed that the ubiquitin ligase activity of Rsp5p is essential for its function in mitochondrial inheritance. A second mutation, smm2, which also suppressed mdm1-252 defects, but did not cause aberrant mitochondrial distribution and morphology, mapped to BUL1, encoding a protein interacting with Rsp5p. These results indicate that protein ubiquitination mediated by Rsp5p plays an essential role in mitochondrial inheritance, and reveal a novel function for protein ubiquitination.

Indexed as

Adaptor Proteins, Signal TransducingCell Cycle ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesAmino Acid SubstitutionCarrier ProteinsEndosomal Sorting Complexes Required for TransportFungal ProteinsGene ExpressionGenes, EssentialGenes, FungalGenes, SuppressorGenetic Complementation TestIntermediate Filament ProteinsLigasesMitochondriaAdaptor Proteins, Signal TransducingBUL1 protein, S cerevisiaeCarrier ProteinsCell Cycle ProteinsEndosomal Sorting Complexes Required for TransportFungal ProteinsIntermediate Filament ProteinsLigasesMDM1 protein, S cerevisiaeRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID10366593
PMCPMC2133147
OpenAlexW2161177314

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.