Evidence map›Paper›PMID 22303011›Full record

ArticleThe Journal of biological chemistry2012

Crystal structure of mitochondrial fission complex reveals scaffolding function for mitochondrial division 1 (Mdv1) coiled coil.

Yan Zhang, Nickie C Chan, Huu B Ngo, Harry Gristick, David C Chan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Mitochondrial Quality Control.Advances in experimental medicine and biology · 2025
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  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Molecular mechanisms for mitochondrial adaptation to exercise training in skeletal muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Review
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  13. Article
  14. Article
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  16. Article
  17. Article
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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

5 authors at 2 institutions in 1 country.

Yan ZhangDivision of Biology, California Institute of Technology, Pasadena, California 91125.
Nickie C ChanDivision of Biology, California Institute of Technology, Pasadena, California 91125; Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California 91125.
Huu B NgoDivision of Biology, California Institute of Technology, Pasadena, California 91125.
Harry GristickDivision of Biology, California Institute of Technology, Pasadena, California 91125.
David C ChanDivision of Biology, California Institute of Technology, Pasadena, California 91125; Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California 91125. Electronic address: dchan@caltech.edu.
California Institute of Technology · USHoward Hughes Medical Institute · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
Mitochondrial Fusion: Analysis of Fzo FunctionR01GM062967 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CHAN, DAVID C · 2001 to 2014
$3.7M
Structural and mechanistic studies of mitochondrial fissionR01GM083121 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CHAN, DAVID C · 2007 to 2010
$1.4M
Howard Hughes Medical InstituteNCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NIGMS NIH HHS GM062967NIGMS NIH HHS GM083121NIGMS NIH HHS R01 GM062967NIGMS NIH HHS R01 GM083121
6 · The paper itself

Abstract

The mitochondrial fission machinery is best understood in the yeast Saccharomyces cerevisiae, where Fis1, Mdv1, and Dnm1 are essential components. Fis1 is a mitochondrial outer membrane protein that recruits the dynamin-related GTPase Dnm1 during the fission process. This recruitment occurs via Mdv1, which binds both Fis1 and Dnm1 and therefore functions as a molecular adaptor linking the two molecules. Mdv1 has a modular structure, consisting of an N-terminal extension that binds Fis1, a central coiled coil for dimerization, and a C-terminal WD40 repeat region that binds Dnm1. We have solved the crystal structure of a dimeric Mdv1-Fis1 complex that contains both the N-terminal extension and coiled-coil regions of Mdv1. Consistent with previous studies, Mdv1 binds Fis1 through a U-shaped helix-loop-helix motif, and dimerization of the Mdv1-Fis1 complex is mediated by the antiparallel coiled coil of Mdv1. However, the complex is surprisingly compact and rigid due to two additional contacts mediated by the surface of the Mdv1 coiled coil. The coiled coil packs against both Fis1 and the second helix of the Mdv1 helix-loop-helix motif. Mutational analyses showed that these contacts are important for mitochondrial fission activity. These results indicate that, in addition to dimerization, the unusually long Mdv1 coiled coil serves a scaffolding function to stabilize the Mdv1-Fis1 complex.

Indexed as

Protein FoldingProtein MultimerizationAdaptor Proteins, Signal TransducingCrystallography, X-RayGTP PhosphohydrolasesHelix-Loop-Helix MotifsMitochondriaMitochondrial ProteinsMultiprotein ComplexesProtein BindingProtein Structure, QuaternaryProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingDNM1 protein, S cerevisiaeFIS1 protein, S cerevisiaeGTP PhosphohydrolasesMDV1 protein, S cerevisiaeMitochondrial ProteinsMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID22303011
PMCPMC3323041
OpenAlexW2071440075

What OpenQuestion holds

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LicenceCC BY-NC
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.