Evidence map›Paper›PMID 17893242›Full record

ArticleThe Journal of cell biology2007

Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion.

David K Hwang, Steven M Claypool, Danielle Leuenberger, Heather L Tienson, Carla M Koehler

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 48 citations in OpenAlex.

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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 at 2 institutions in 2 countries.

David K HwangDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Steven M Claypool
Danielle Leuenberger
Heather L Tienson
Carla M Koehler
Laboratoire de Biochimie · FRUniversity of California, Los Angeles · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Biogenesis of the mitochondrial inner membrane diversity supplementR01GM061721 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KOEHLER, CARLA M · 2000 to 2025
$8.1M
NIGMS NIH HHS GM07185NIGMS NIH HHS R01 GM061721NIGMS NIH HHS R01 GM61721NIGMS NIH HHS T32 GM007185
6 · The paper itself

Abstract

Tim54p, a component of the inner membrane TIM22 complex, does not directly mediate the import of inner membrane substrates but is required for assembly/stability of the 300-kD TIM22 complex. In addition, Deltatim54 yeast exhibit a petite-negative phenotype (also observed in yeast harboring mutations in the F1Fo ATPase, the ADP/ATP carrier, mitochondrial morphology components, or the i-AAA protease, Yme1p). Interestingly, other import mutants in our strain background are not petite-negative. We report that Tim54p is not involved in maintenance of mitochondrial DNA or mitochondrial morphology. Rather, Tim54p mediates assembly of an active Yme1p complex, after Yme1p is imported via the TIM23 pathway. Defective Yme1p assembly is likely the major contributing factor for the petite-negativity in strains lacking functional Tim54p. Thus, Tim54p has two independent functions: scaffolding/stability for the TIM22 membrane complex and assembly of Yme1p into a proteolytically active complex. As such, Tim54p links protein import, assembly, and turnover pathways in the mitochondrion.

Indexed as

Protein Processing, Post-TranslationalAdenosine TriphosphatasesATP-Dependent ProteasesDNA, MitochondrialGene ExpressionGlucoseMembrane Transport ProteinsMicrobial ViabilityMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsModels, BiologicalMutationProtein BindingProtein TransportAdenosine TriphosphatasesATP-Dependent ProteasesDNA, MitochondrialGlucoseMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsSaccharomyces cerevisiae ProteinsTIM22 protein, S cerevisiaeTIM54 protein, S cerevisiaeYME1 protein, S cerevisiae

Identifiers

PMID17893242
PMCPMC2064651
OpenAlexW2109931939

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.