Evidence map›Paper›PMID 30409808›Full record

ArticleScience (New York, N.Y.)2018

Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway.

Jeong-Mok Kim, Ok-Hee Seok, Shinyeong Ju, Ji-Eun Heo, Jeonghun Yeom, Da-Som Kim, Joo-Yeon Yoo, Alexander Varshavsky, Cheolju Lee, Cheol-Sang Hwang

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.6field-weighted citation impact, top 5% 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

50 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Formylation facilitates the reduction of oxidized initiator methionines.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 2 countries.

Jeong-Mok KimDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.ORCID 0000-0002-7223-248X
Ok-Hee SeokDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.
Shinyeong JuCenter for Theragnosis, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.ORCID 0000-0001-5483-4690
Ji-Eun HeoDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.
Jeonghun YeomCenter for Theragnosis, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.
Da-Som KimDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.
Joo-Yeon YooDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea.ORCID 0000-0001-5942-3989
Alexander VarshavskyDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA.ORCID 0000-0002-4011-258X
Cheolju LeeCenter for Theragnosis, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea. cshwang@postech.ac.kr clee270@kist.re.kr.ORCID 0000-0001-8482-4696
Cheol-Sang HwangDepartment of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea. cshwang@postech.ac.kr clee270@kist.re.kr.ORCID 0000-0002-0105-5957
Pohang University of Science and Technology · KRBio-Medical Science (South Korea) · KRCalifornia Institute of Technology · USHanyang University · KRKyung Hee University · KR

Funding

The Functions, Mechanisms, and Regulation of N-Terminal ArginylationR01GM031530 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALEXANDER J VARSHAVSKY · 1985 to 2026
$14.5M
Ubiquitin Ligases, Mechanisms and Functions of the N-End Rule PathwayR01DK039520 · NIDDK · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI VARSHAVSKY, ALEXANDER J · 1988 to 2025
$10.0M
NIDDK NIH HHS R01 DK039520NIGMS NIH HHS R01 GM031530
6 · The paper itself

Abstract

In bacteria, nascent proteins bear the pretranslationally generated N-terminal (Nt) formyl-methionine (fMet) residue. Nt-fMet of bacterial proteins is a degradation signal, termed fMet/N-degron. By contrast, proteins synthesized by cytosolic ribosomes of eukaryotes were presumed to bear unformylated Nt-Met. Here we found that the yeast formyltransferase Fmt1, although imported into mitochondria, could also produce Nt-formylated proteins in the cytosol. Nt-formylated proteins were strongly up-regulated in stationary phase or upon starvation for specific amino acids. This up-regulation strictly required the Gcn2 kinase, which phosphorylates Fmt1 and mediates its retention in the cytosol. We also found that the Nt-fMet residues of Nt-formylated proteins act as fMet/N-degrons and identified the Psh1 ubiquitin ligase as the recognition component of the eukaryotic fMet/N-end rule pathway, which destroys Nt-formylated proteins.

Indexed as

ProteolysisAmino AcidsAzidesCold TemperatureCytosolHydroxymethyl and Formyl TransferasesMetabolic Networks and PathwaysMitochondriaN-FormylmethioninePeptide Elongation FactorsPhosphorylationProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesUp-RegulationAmino AcidsAzidesGCN2 protein, S cerevisiaeHydroxymethyl and Formyl Transferasesmethionyl-tRNA formyltransferaseN-FormylmethioninePeptide Elongation FactorsProtein Serine-Threonine KinasesPsh1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID30409808
PMCPMC6551516
OpenAlexW2900397067

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.