Evidence map›Paper›PMID 29029422›Full record

ArticleOncotarget2017

Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma.

Suliman Boulos, Min Chul Park, Marian Zeibak, Shen Yun Foo, Yoon Kyung Jeon, Young Tae Kim, Alex Motzik, Sagi Tshori, Tamar Hamburger, Sunghoon Kim and 2 more

Erratum issuedOpen access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. The pLysRS-ApInternational journal of molecular sciences · 2021
    Review
  6. Article
  7. Roles of Aminoacyl-tRNA Synthetases in Cancer.Frontiers in cell and developmental biology · 2020
    Review
  8. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 3 countries.

Suliman BoulosDepartment of Oncology, Hadassah Hebrew University Hospital, Jerusalem, Israel.
Min Chul ParkMedicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea.
Marian ZeibakDepartment of Biochemistry and Molecular Biology, Institute for Medical Research Israel-Canada, The Hebrew University of Jerusalem, Jerusalem, Israel.
Shen Yun FooNUS-HUJ-CREATE Cellular & Molecular Mechanisms of Inflammation Program, Department of Microbiology and Immunology, National University of Singapore, Singapore.
Yoon Kyung JeonDepartment of Pathology, Seoul National University Hospital, Seoul, Korea.
Young Tae KimDepartment of Thoracic and Cardiovascular Surgery, Seoul National University Hospital, Seoul, Korea.
Alex MotzikDepartment of Biochemistry and Molecular Biology, Institute for Medical Research Israel-Canada, The Hebrew University of Jerusalem, Jerusalem, Israel.
Sagi TshoriKaplan Medical Center, Rehovot, Israel.
Tamar HamburgerSharett Institute of Oncology, Hadassah Hebrew University Hospital, Jerusalem, Israel.
Sunghoon KimMedicinal Bioconvergence Research Center, Seoul National University, Seoul, Korea.
Hovav NechushtanDepartment of Oncology, Hadassah Hebrew University Hospital, Jerusalem, Israel.
Ehud RazinDepartment of Biochemistry and Molecular Biology, Institute for Medical Research Israel-Canada, The Hebrew University of Jerusalem, Jerusalem, Israel.
Hebrew University of Jerusalem · ILNational University of Singapore · SGSeoul National University · KRSeoul National University Hospital · KRHadassah Medical Center · ILKaplan Medical Center · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It has been shown that various tRNA synthetases exhibit non-canonical activities unrelated to their original role in translation. We have previously described a signal transduction pathway in which serine 207 phosphorylated lysyl-tRNA synthetase (P-s207 LysRS) is released from the cytoplasmic multi-tRNA synthetase complex (MSC) into the nucleus, where it activates the transcription factor MITF in stimulated cultured mast cells and cardiomyocytes. Here we describe a similar transformation of LysRS due to EGFR signaling activation in human lung cancer. Our data shows that activation of the EGFR results in phosphorylation of LysRS at position serine 207, its release from the MSC and translocation to the nucleus. We then generated a P-s207 LysRS rabbit polyclonalantibody and tested 242 tissue micro-array samples derived from non-small-cell lung cancer patients. Highly positive nuclear staining for P-s207 LysRS was noted in patients with EGFR mutations as compared to WT EGFR patients and was associated with improved mean disease-free survival (DFS). In addition, patients with mutated EGFR and negative lymph node metastases had better DFS when P-s207 LysRS was present in the nucleus. The data presented strongly suggests functional and prognostic significance of P-s207 LysRS in non-small-cell lung cancer.

Indexed as

EGFRLysRSmulti-synthetase complexnon-small-cell lung cancerP-s207 LysRS

Identifiers

PMID29029422
PMCPMC5630322
OpenAlexW2619602420

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.