Evidence map›Paper›PMID 31522117›Full record

ArticleiScience2019

Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region.

Takahiro Yoshinaka, Hidetaka Kosako, Takuma Yoshizumi, Ryo Furukawa, Yu Hirano, Osamu Kuge, Taro Tamada, Takumi Koshiba

Open access · goldAbstract read
In one paragraph

Article in iScience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 98 citations in OpenAlex.

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  14. Heliyon · 2023
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  19. Proximity Labeling in Plants.Annual review of plant biology · 2023
    Review
  20. Dodecamer assembly of a metazoan AAAScience advances · 2023
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1 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 1 country.

Takahiro YoshinakaDepartment of Biology, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan.
Hidetaka KosakoDivision of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Tokushima University, Tokushima 770-8503, Japan.
Takuma YoshizumiDepartment of Biology, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan.
Ryo FurukawaDepartment of Biology, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan.
Yu HiranoQuantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, Ibaraki 319-1106, Japan.
Osamu KugeDepartment of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan.
Taro TamadaQuantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, Ibaraki 319-1106, Japan.
Takumi KoshibaDepartment of Biology, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan; Department of Chemistry, Faculty of Science, Fukuoka University, Fukuoka 814-0180, Japan. Electronic address: koshiba@kyudai.jp.
Kyushu University · JPNational Institutes for Quantum Science and Technology · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The coiled-coil motif mediates subunit oligomerization and scaffolding and underlies several fundamental biologic processes. Prohibitins (PHBs), mitochondrial inner membrane proteins involved in mitochondrial homeostasis and signal transduction, are predicted to have a coiled-coil motif, but their structural features are poorly understood. Here we solved the crystal structure of the heptad repeat (HR) region of PHB2 at 1.7-Å resolution, showing that it assembles into a dimeric, antiparallel coiled-coil with a unique negatively charged area essential for the PHB interactome in mitochondria. Disruption of the HR coiled-coil abolishes well-ordered PHB complexes and the mitochondrial tubular networks accompanying PHB-dependent signaling. Using a proximity-dependent biotin identification (BioID) technique in live cells, we mapped a number of mitochondrial intermembrane space proteins whose association with PHB2 relies on the HR coiled-coil region. Elucidation of the PHB complex structure in mitochondria provides insight into essential PHB interactomes required for mitochondrial dynamics as well as signal transduction.

Indexed as

Cell BiologyMolecular BiologyStructural Biology

Identifiers

PMID31522117
PMCPMC6745515
OpenAlexW2971840884

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.