Evidence map›Paper›PMID 18426906›Full record

ArticleMolecular and cellular biology2008

Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering.

Dirk Schiller, Yu Chin Cheng, Qinglian Liu, William Walter, Elizabeth A Craig

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

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  16. Mechanisms of protein sorting in mitochondria.Cold Spring Harbor perspectives in biology · 2012
    Review
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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 1 country.

Dirk SchillerDepartment of Biochemistry, 433 Babcock Drive, University of Wisconsin-Madison, Madison, WI 53726, USA.
Yu Chin Cheng
Qinglian Liu
William Walter
Elizabeth A Craig
Abbott Fund · USUniversity of Wisconsin–Madison · US

Funding

NIGMS NIH HHS GM278709
6 · The paper itself

Abstract

Translocation of proteins from the cytosol across the mitochondrial inner membrane is driven by the action of the import motor, which is associated with the translocon on the matrix side of the membrane. It is well established that an essential peripheral membrane protein, Tim44, tethers mitochondrial Hsp70 (mtHsp70), the core of the import motor, to the translocon. This Tim44-mtHsp70 interaction, which can be recapitulated in vitro, is destabilized by binding of mtHsp70 to a substrate polypeptide. Here we report that the N-terminal 167-amino-acid segment of mature Tim44 is sufficient for both interaction with mtHsp70 and destabilization of a Tim44-mtHsp70 complex caused by client protein binding. Amino acid alterations within a 30-amino-acid segment affected both the release of mtHsp70 upon peptide binding and the interaction of Tim44 with the translocon. Our results support the idea that Tim44 plays multiple roles in mitochondrial protein import by recruiting Ssc1 and its J protein cochaperone to the translocon and coordinating their interactions to promote efficient protein translocation in vivo.

Indexed as

Amino AcidsAmino Acid SequenceAmino Acid SubstitutionCalcium-Transporting ATPasesDNA Mutational AnalysisMembrane Transport ProteinsMitochondriaMitochondrial ADP, ATP TranslocasesMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMolecular ChaperonesMolecular Sequence DataMutant ProteinsProtein BindingProtein TransportAmino AcidsCalcium-Transporting ATPasesMembrane Transport ProteinsMitochondrial ADP, ATP TranslocasesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMolecular ChaperonesMutant ProteinsSaccharomyces cerevisiae ProteinsSSC1 protein, S cerevisiaeTIM23 protein, S cerevisiaeTIM44 protein, S cerevisiae

Identifiers

PMID18426906
PMCPMC2447135
OpenAlexW2153722941

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.