Evidence map›Paper›PMID 16790494›Full record

ArticleMolecular biology of the cell2006

The novel F-box protein Mfb1p regulates mitochondrial connectivity and exhibits asymmetric localization in yeast.

Noriko Kondo-Okamoto, Kentaro Ohkuni, Katsumi Kitagawa, J Michael McCaffery, Janet M Shaw, Koji Okamoto

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 14% 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, 43 citations in OpenAlex.

  1. Review
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  8. Article
  9. Mitochondrial anchors: Positioning mitochondria and more.Biochemical and biophysical research communications · 2018
    Review
  10. Mitochondrial Tethers and Their Impact on Lifespan in Budding Yeast.Frontiers in cell and developmental biology · 2017
    Review
  11. Article
  12. Article
  13. 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

6 authors at 3 institutions in 1 country.

Noriko Kondo-OkamotoDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.
Kentaro Ohkuni
Katsumi Kitagawa
J Michael McCaffery
Janet M Shaw
Koji Okamoto
University of Utah · USSt. Jude Children's Research Hospital · USImaging Center · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
REGULATION OF MITOCHONDRIAL INHERITANCE IN YEASTR01GM053466 · NIGMS · UNIVERSITY OF UTAH · PI SHAW, JANET M. · 1996 to 2013
$4.6M
Kinetochore Function and Cell Cycle Progression RevisionR01GM068418 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI KITAGAWA, KATSUMI · 2003 to 2012
$2.5M
Zeiss LSM 510 META Confocal MicroscopeS10RR019409 · NCRR · JOHNS HOPKINS UNIVERSITY · PI MCCAFFERY, J. MICHAEL · 2004 to 2004
$485k
NCI NIH HHS 5-P30CA42014NCI NIH HHS CA-21765NCI NIH HHS P30 CA021765NCI NIH HHS P30 CA042014NCRR NIH HHS S10 RR019409NIGMS NIH HHS GM-53466NIGMS NIH HHS GM-68418NIGMS NIH HHS R01 GM053466NIGMS NIH HHS R01 GM068418
6 · The paper itself

Abstract

Although it is clear that mitochondrial morphogenesis is a complex process involving multiple proteins in eukaryotic cells, little is known about regulatory molecules that modulate mitochondrial network formation. Here, we report the identification of a new yeast mitochondrial morphology gene called MFB1 (YDR219C). MFB1 encodes an F-box protein family member, many of which function in Skp1-Cdc53/Cullin-F-box protein (SCF) ubiquitin ligase complexes. F-box proteins also act in non-SCF complexes whose functions are not well understood. Although cells lacking Mfb1p contain abnormally short mitochondrial tubules, Mfb1p is not essential for known pathways that determine mitochondrial morphology and dynamics. Mfb1p is peripherally associated with the mitochondrial surface. Coimmunoprecipitation assays reveal that Mfb1p interacts with Skp1p in an F-box-dependent manner. However, Mfb1p does not coimmunoprecipitate with Cdc53p. The F-box motif is not essential for Mfb1p-mediated mitochondrial network formation. These observations suggest that Mfb1p acts in a complex lacking Cdc53p required for mitochondrial morphogenesis. During budding, Mfb1p asymmetrically localizes to mother cell mitochondria. By contrast, Skp1p accumulates in the daughter cell cytoplasm. Mfb1p mother cell-specific asymmetry depends on the F-box motif, suggesting that Skp1p down-regulates Mfb1p mitochondrial association in buds. We propose that Mfb1p operates in a novel pathway regulating mitochondrial tubular connectivity.

Indexed as

Cell PolarityAmino Acid MotifsAmino Acid SequenceCytoplasmF-Box ProteinsMitochondriaMolecular Sequence DataMutationPeptide HydrolasesProtein BindingProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsS-Phase Kinase-Associated ProteinsStem CellsF-Box ProteinsMfb1 protein, S cerevisiaePeptide HydrolasesSaccharomyces cerevisiae ProteinsS-Phase Kinase-Associated Proteins

Identifiers

PMID16790494
PMCPMC1593157
OpenAlexW2130677875

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.