Evidence map›Paper›PMID 14517324›Full record

ArticleMolecular biology of the cell2003

The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria.

Kara L Cerveny, Robert E Jensen

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

48 citing papers in PubMed, 106 citations in OpenAlex.

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  16. Review
  17. Mechanisms of mitochondrial fission and fusion.Cold Spring Harbor perspectives in biology · 2013
    Review
  18. Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Review
  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

2 authors at 1 institution in 1 country.

Kara L CervenyDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Robert E Jensen
Johns Hopkins University · US

Funding

MITOCHONDRIAL DYNAMICS-MORPHOLOGY/DIVISION/SEGREGATIONR01GM054021 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JENSEN, ROBERT E · 1996 to 2008
$2.7M
NIGMS NIH HHS R01 GM054021NIGMS NIH HHS R01-GM54021-06
6 · The paper itself

Abstract

The Net2, Fis1, and Dnm1 proteins are required for the division of mitochondria in the yeast Saccharomyces cerevisiae. Net2p has an amino-terminal region that contains predicted coiled-coil motifs and a carboxyl-terminal domain composed of WD-40 repeats. We found that the amino-terminal part of Net2p interacts with Fis1p, whereas the carboxyl-terminal region interacts with both Dnm1p and Fis1p. Overproduction of either domain of Net2p in yeast cells poisons mitochondrial fission, and the dominant-negative effect caused by the WD-repeats of Net2p is suppressed by increased levels of Dnm1p. Point mutations in the WD-region of Net2p or in the GTPase region of Dnm1p disrupt the normal Net2p-Dnm1p interaction, causing Net2p to lose its normal punctate distribution. Our results suggest that Dnm1p interacts with the WD-repeats of Net2p and in a GTP-dependent manner recruits Net2p to sites of mitochondrial division. Furthermore, our results indicate that Net2p is required for proper assembly of the mitochondrial fission components to regulate organelle division.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceCarrier ProteinsCell CompartmentationGTP PhosphohydrolasesMicroscopy, FluorescenceMitochondriaMitochondrial ProteinsMolecular Sequence DataPlasmidsProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTwo-Hybrid System TechniquesAdaptor Proteins, Signal TransducingCarrier ProteinsDNM1 protein, S cerevisiaeFIS1 protein, S cerevisiaeGTP PhosphohydrolasesMDV1 protein, S cerevisiaeMitochondrial ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID14517324
PMCPMC207005
OpenAlexW2140008017

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.