Evidence map›Paper›PMID 28611052›Full record

ArticleThe Journal of cell biology2017

Caspase-8 controls the secretion of inflammatory lysyl-tRNA synthetase in exosomes from cancer cells.

Sang Bum Kim, Hye Rim Kim, Min Chul Park, Seongmin Cho, Peter C Goughnour, Daeyoung Han, Ina Yoon, YounHa Kim, Taehee Kang, Eunjoo Song and 7 more

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.5field-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

63 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
  2. The theory of the inflammatory ecosystem.Science China. Life sciences · 2026
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3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors at 5 institutions in 2 countries.

Sang Bum KimMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea.
Hye Rim KimMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea.
Min Chul ParkMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea.
Seongmin ChoMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea.
Peter C GoughnourMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea.ORCID 0000-0002-5126-0270
Daeyoung HanMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea.
Ina YoonMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea.
YounHa KimMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea.
Taehee KangMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea.
Eunjoo SongGraduate School of Nanoscience and Technology, Korea Advanced Institute of Science and Technology, Daejeon, South Korea.
Pilhan KimGraduate School of Nanoscience and Technology, Korea Advanced Institute of Science and Technology, Daejeon, South Korea.
Hyosun ChoiBK21 Plus Program, Department of Senior Healthcare, Graduate School, Eulji University, Daejeon, South Korea.
Ji Young MunBK21 Plus Program, Department of Senior Healthcare, Graduate School, Eulji University, Daejeon, South Korea.
Chihong SongNational Institute for Physiological Sciences, Okazaki, Japan.
Sangmin LeeDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, South Korea.
Hyun Suk JungDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, South Korea.
Sunghoon KimMedicinal Bioconvergence Research Center, Seoul National University, Suwon, South Korea sungkim@snu.ac.kr.ORCID 0000-0002-1570-3230
Seoul National University · KREulji University · KRKangwon National University · KRKorea Advanced Institute of Science and Technology · KRNational Institute for Physiological Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases (ARSs), enzymes that normally control protein synthesis, can be secreted and have different activities in the extracellular space, but the mechanism of their secretion is not understood. This study describes the secretion route of the ARS lysyl-tRNA synthetase (KRS) and how this process is regulated by caspase activity, which has been implicated in the unconventional secretion of other proteins. We show that KRS is secreted from colorectal carcinoma cells within the lumen of exosomes that can trigger an inflammatory response. Caspase-8 cleaved the N-terminal of KRS, thus exposing a PDZ-binding motif located in the C terminus of KRS. Syntenin bound to the exposed PDZ-binding motif of KRS and facilitated the exosomic secretion of KRS dissociated from the multi-tRNA synthetase complex. KRS-containing exosomes released by cancer cells induced macrophage migration, and their secretion of TNF-α and cleaved KRS made a significant contribution to these activities, which suggests a novel mechanism by which caspase-8 may promote inflammation.

Indexed as

AnimalsCaspase 8ChemotaxisColorectal NeoplasmsExosomesHCT116 CellsHumansInflammation MediatorsLysine-tRNA LigaseMacrophagesMiceMultienzyme ComplexesPDZ DomainsProtein BindingRAW 264.7 CellsRNA InterferenceCASP8 protein, humanCaspase 8Inflammation MediatorsKARS1 protein, humanLysine-tRNA LigaseMultienzyme ComplexesSynteninsTumor Necrosis Factor-alpha

Identifiers

PMID28611052
PMCPMC5496609
OpenAlexW2625552877

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.