Evidence map›Paper›PMID 16790493›Full record

ArticleMolecular biology of the cell2006

Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import.

Michelle R Gallas, Mary K Dienhart, Rosemary A Stuart, Roy M Long

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

37 citing papers in PubMed, 60 citations in OpenAlex.

  1. Mitochondrial membrane remodeling in stress adaptation: Lipid control of organelle quality.Protein science : a publication of the Protein Society · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Crosstalk between Mitochondrial Protein Import and Lipids.International journal of molecular sciences · 2022
    Review
  6. Biallelic variants inHGG advances · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Role of Cardiolipin in Mitochondrial Signaling Pathways.Frontiers in cell and developmental biology · 2017
    Review
  14. Biosynthesis, remodeling and turnover of mitochondrial cardiolipin.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  15. Article
  16. Lipid topogenesis--35years on.Biochimica et biophysica acta · 2016
    Review
  17. How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016
    Review
  18. Article
  19. Review
  20. Review
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.

Michelle R GallasDepartment of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, WI 53226, USA.
Mary K Dienhart
Rosemary A Stuart
Roy M Long
Marquette University · USMedical College of Wisconsin · US

Funding

RNA LOCALIZATION IN S.CEREVISIAER01GM060392 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI LONG, ROY M · 2000 to 2004
$1.1M
NIGMS NIH HHS R01 GM060392
6 · The paper itself

Abstract

Many mitochondrial proteins are encoded by nuclear genes and after translation in the cytoplasm are imported via translocases in the outer and inner membranes, the TOM and TIM complexes, respectively. Here, we report the characterization of the mitochondrial protein, Mmp37p (YGR046w) and demonstrate its involvement in the process of protein import into mitochondria. Haploid cells deleted of MMP37 are viable but display a temperature-sensitive growth phenotype and are inviable in the absence of mitochondrial DNA. Mmp37p is located in the mitochondrial matrix where it is peripherally associated with the inner membrane. We show that Mmp37p has a role in the translocation of proteins across the mitochondrial inner membrane via the TIM23-PAM complex and further demonstrate that substrates containing a tightly folded domain in close proximity to their mitochondrial targeting sequences display a particular dependency on Mmp37p for mitochondrial import. Prior unfolding of the preprotein, or extension of the region between the targeting signal and the tightly folded domain, relieves their dependency for Mmp37p. Furthermore, evidence is presented to show that Mmp37 may affect the assembly state of the TIM23 complex. On the basis of these findings, we hypothesize that the presence of Mmp37p enhances the early stages of the TIM23 matrix import pathway to ensure engagement of incoming preproteins with the mtHsp70p/PAM complex, a step that is necessary to drive the unfolding and complete translocation of the preprotein into the matrix.

Indexed as

Cell SurvivalChaperonin 60ChaperoninsDNA, MitochondrialHaploidyHeat-Shock ProteinsHSP40 Heat-Shock ProteinsMeiosisMembrane ProteinsMembrane Transport ProteinsMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsOpen Reading FramesChaperonin 60ChaperoninsDNA, MitochondrialHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP60 protein, S cerevisiaeMDJ1 protein, S cerevisiaeMembrane ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsProtein PrecursorsSaccharomyces cerevisiae ProteinsTAM41 protein, S cerevisiaeTIM23 protein, S cerevisiae

Identifiers

PMID16790493
PMCPMC1556384
OpenAlexW1985380517

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.