Evidence map›Paper›PMID 11564892›Full record

ArticleMolecular and cellular biology2001

Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins.

A Geissler, J Rassow, N Pfanner, W Voos

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 72 citations in OpenAlex.

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  19. Age-dependent deficiency in import of mitochondrial DNA glycosylases required for repair of oxidatively damaged bases.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  20. The substrate binding domain of DnaK facilitates slow protein refolding.Proceedings of the National Academy of Sciences of the United States of America · 2002
    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

4 authors at 2 institutions in 1 country.

A GeisslerInstitut für Biochemie und Molekularbiologie, Universität Freiburg, D-79104 Freiburg, Germany.
J Rassow
N Pfanner
W Voos
University of Freiburg · DEUniversity of Hohenheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial heat shock protein Hsp70 (mtHsp70) is essential for driving translocation of preproteins into the matrix. Two models, trapping and pulling by mtHsp70, are discussed, but positive evidence for either model has not been found so far. We have analyzed a mutant mtHsp70, Ssc1-2, that shows a reduced interaction with the membrane anchor Tim44, but an enhanced trapping of preproteins. Unexpectedly, at a low inner membrane potential, ssc1-2 mitochondria imported loosely folded preproteins more efficiently than wild-type mitochondria. The import of a tightly folded preprotein, however, was not increased in ssc1-2 mitochondria. Thus, enhanced trapping by mtHsp70 stimulates the import of loosely folded preproteins and reduces the dependence on the import-driving activity of the membrane potential, directly demonstrating that trapping is one of the molecular mechanisms of mtHsp70 action.

Indexed as

Heat-Shock ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsSaccharomyces cerevisiae ProteinsCalcium-Transporting ATPasesCarrier ProteinsCell MembraneCisplatinCross-Linking ReagentsDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelFungal ProteinsHSP70 Heat-Shock ProteinsMembrane PotentialsMembrane ProteinsMitochondriaCalcium-Transporting ATPasesCarrier ProteinsCisplatinCross-Linking ReagentsFungal ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsMembrane ProteinsMembrane Transport ProteinsMGE1 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMolecular ChaperonesSaccharomyces cerevisiae ProteinsSSC1 protein, S cerevisiaeTIM44 protein, S cerevisiae

Identifiers

PMID11564892
PMCPMC99885
OpenAlexW2171032298

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.