Evidence map›Paper›PMID 14981098›Full record

ArticleThe Journal of cell biology2004

Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids.

Matthew J Youngman, Alyson E Aiken Hobbs, Shawn M Burgess, Maithreyan Srinivasan, Robert E Jensen

Abstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
–field-weighted citation impact
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

68 citing papers in PubMed.

  1. Article
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  5. InJournal of fungi (Basel, Switzerland) · 2023
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8 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

5 authors.

Matthew J YoungmanDepartment of Cell Biology, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, USA.
Alyson E Aiken Hobbs
Shawn M Burgess
Maithreyan Srinivasan
Robert E Jensen

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
Zebrafish targeted mutagenesis and functional genomicsZIAHG000183 · NHGRI · NATIONAL HUMAN GENOME RESEARCH INSTITUTE · PI BURGESS, SHAWN M · 2009 to 2025
$16.7M
Insertional mutagenesis and ear developmentZ01HG000183 · NHGRI · NATIONAL HUMAN GENOME RESEARCH INSTITUTE · PI BURGESS, SHAWN M · 2001 to 2008
$3.3M
MITOCHONDRIAL DYNAMICS-MORPHOLOGY/DIVISION/SEGREGATIONR01GM054021 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JENSEN, ROBERT E · 1996 to 2008
$2.7M
NIGMS NIH HHS 2T32-GM07445NIGMS NIH HHS R01 GM054021NIGMS NIH HHS R01-GM54021NIGMS NIH HHS T32 GM007445
6 · The paper itself

Abstract

The mitochondrial outer membrane protein, Mmm1p, is required for normal mitochondrial shape in yeast. To identify new morphology proteins, we isolated mutations incompatible with the mmm1-1 mutant. One of these mutants, mmm2-1, is defective in a novel outer membrane protein. Lack of Mmm2p causes a defect in mitochondrial shape and loss of mitochondrial DNA (mtDNA) nucleoids. Like the Mmm1 protein (Aiken Hobbs, A.E., M. Srinivasan, J.M. McCaffery, and R.E. Jensen. 2001. J. Cell Biol. 152:401-410.), Mmm2p is located in dot-like particles on the mitochondrial surface, many of which are adjacent to mtDNA nucleoids. While some of the Mmm2p-containing spots colocalize with those containing Mmm1p, at least some of Mmm2p is separate from Mmm1p. Moreover, while Mmm2p and Mmm1p both appear to be part of large complexes, we find that Mmm2p and Mmm1p do not stably interact and appear to be members of two different structures. We speculate that Mmm2p and Mmm1p are components of independent machinery, whose dynamic interactions are required to maintain mitochondrial shape and mtDNA structure.

Indexed as

Cell DivisionCell MembraneDNA, MitochondrialMacromolecular SubstancesMembrane ProteinsMitochondriaMitochondrial ProteinsNucleic Acid ConformationRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubcellular FractionsDNA, MitochondrialMacromolecular SubstancesMembrane ProteinsMitochondrial ProteinsMMM1 protein, S cerevisiaeMMM2 protein, S cerevisiaeRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID14981098
PMCPMC2172170

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.