Evidence map›Paper›PMID 27496949›Full record

ArticleThe Journal of biological chemistry2016

A Targeted Mutation Identified through pKa Measurements Indicates a Postrecruitment Role for Fis1 in Yeast Mitochondrial Fission.

Marijke Koppenol-Raab, Megan Cleland Harwig, Ammon E Posey, John M Egner, Kevin R MacKenzie, R Blake Hill

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Ecm19 coordinates mitochondrial fission and cellular redox homeostasis.Redox report : communications in free radical research · 2025
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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.

Marijke Koppenol-RaabFrom the Department of Biology and.
Megan Cleland Harwigthe Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, and.
Ammon E PoseyFrom the Department of Biology and the Program in Molecular Biophysics, Johns Hopkins University, Baltimore, Maryland 21218.
John M Egnerthe Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, and.
Kevin R MacKenziethe Department of Pathology, Baylor College of Medicine, Houston, Texas 77030.
R Blake Hillthe Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, and rbhill@mcw.edu.
Medical College of Wisconsin · USBaylor College of Medicine · USJohns Hopkins University · US

Funding

Structural Biology of Mitochondrial FissionR01GM067180 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI HILL, R BLAKE · 2004 to 2022
$6.0M
NIGMS NIH HHS R01 GM067180
6 · The paper itself

Abstract

The tail-anchored protein Fis1 is implicated as a passive tether in yeast mitochondrial fission. We probed the functional role of Fis1 Glu-78, whose elevated side chain pKa suggests participation in protein interactions. Fis1 binds partners Mdv1 or Dnm1 tightly, but mutation E78A weakens Fis1 interaction with Mdv1, alters mitochondrial morphology, and abolishes fission in a growth assay. In fis1Δ rescue experiments, Fis1-E78A causes a novel localization pattern in which Dnm1 uniformly coats the mitochondria. By contrast, Fis1-E78A at lower expression levels recruits Dnm1 into mitochondrial punctate structures but fails to support normal fission. Thus, Fis1 makes multiple interactions that support Dnm1 puncta formation and may be essential after this step, supporting a revised model for assembly of the mitochondrial fission machinery. The insights gained by mutating a residue with a perturbed pKa suggest that side chain pKa values inferred from routine NMR sample pH optimization could provide useful leads for functional investigations.

Indexed as

Mutation, MissenseAmino Acid SubstitutionGTP PhosphohydrolasesMitochondriaMitochondrial DynamicsMitochondrial ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNM1 protein, S cerevisiaeFIS1 protein, S cerevisiaeGTP PhosphohydrolasesMitochondrial ProteinsSaccharomyces cerevisiae Proteinsconfocal microscopymacromolecular machinemitochondriamitochondrial dynamicsnuclear magnetic resonance (NMR)pKa measurementsprotein assemblyprotein-protein interactionstructural modeltetratricopeptide repeat (TPR) domains

Identifiers

PMID27496949
PMCPMC5034033
OpenAlexW2496080665

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.