Evidence map›Paper›PMID 27799292›Full record

ArticleMolecular and cellular biology2017

SUMO-Modified FADD Recruits Cytosolic Drp1 and Caspase-10 to Mitochondria for Regulated Necrosis.

Seon-Guk Choi, Hyunjoo Kim, Eun Il Jeong, Ho-June Lee, Sungwoo Park, Song-Yi Lee, Hyeon-Jeong Lee, Seong Won Lee, Chin Ha Chung, Yong-Keun Jung

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  14. Regulation of apoptosis by ubiquitination in liver cancer.American journal of cancer research · 2023
    Review
  15. Review
  16. A Dual Role for FADD in Human Precursor T-Cell Neoplasms.International journal of molecular sciences · 2022
    Article
  17. FADD as a key molecular player in cancer progression.Molecular medicine (Cambridge, Mass.) · 2022
    Review
  18. Article
  19. SUMOylation-Mediated Response to Mitochondrial Stress.International journal of molecular sciences · 2020
    Review
  20. Article
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

10 authors at 1 institution in 1 country.

Seon-Guk ChoiDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Hyunjoo KimDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Eun Il JeongDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Ho-June LeeDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Sungwoo ParkDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Song-Yi LeeDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Hyeon-Jeong LeeDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Seong Won LeeDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Chin Ha ChungDepartment of Biological Science, Seoul National University, Seoul, South Korea.
Yong-Keun JungDepartment of Biological Science, Seoul National University, Seoul, South Korea ykjung@snu.ac.kr.
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fas-associated protein with death domain (FADD) plays a key role in extrinsic apoptosis. Here, we show that FADD is SUMOylated as an essential step during intrinsic necrosis. FADD was modified at multiple lysine residues (K120/125/149) by small ubiquitin-related modifier 2 (SUMO2) during necrosis caused by calcium ionophore A23187 and by ischemic damage. SUMOylated FADD bound to dynamin-related protein 1 (Drp1) in cells both in vitro and in ischemic tissue damage cores, thus promoting Drp1 recruitment by mitochondrial fission factor (Mff) to accomplish mitochondrial fragmentation. Mitochondrial-fragmentation-associated necrosis was blocked by FADD or Drp1 deficiency and SUMO-defective FADD expression. Interestingly, caspase-10, but not caspase-8, formed a ternary protein complex with SUMO-FADD/Drp1 on the mitochondria upon exposure to A23187 and potentiated Drp1 oligomerization for necrosis. Moreover, the caspase-10 L285F and A414V mutants, found in autoimmune lymphoproliferative syndrome and non-Hodgkin lymphoma, respectively, regulated this necrosis. Our study reveals an essential role of SUMOylated FADD in Drp1- and caspase-10-dependent necrosis, providing insights into the mechanism of regulated necrosis by calcium overload and ischemic injury.

Indexed as

AnimalsCaspase 10Cell HypoxiaCytosolDynaminsFas-Associated Death Domain ProteinHEK293 CellsHeLa CellsHumansLysineMice, Inbred C57BLMitochondriaMultiprotein ComplexesMutant ProteinsNecrosisProtein BindingCaspase 10DynaminsFADD protein, humanFadd protein, mouseFas-Associated Death Domain ProteinLysineMultiprotein ComplexesMutant ProteinsRNA, Small InterferingSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO2 protein, humancaspase-10DRP1FADDnecrosisSUMOylation

Identifiers

PMID27799292
PMCPMC5214857
OpenAlexW2543399678

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.