Evidence map›Paper›PMID 26175007›Full record

ArticleNature communications2015

Arginylation regulates purine nucleotide biosynthesis by enhancing the activity of phosphoribosyl pyrophosphate synthase.

Fangliang Zhang, Devang M Patel, Kristen Colavita, Irina Rodionova, Brian Buckley, David A Scott, Akhilesh Kumar, Svetlana A Shabalina, Sougata Saha, Mikhail Chernov and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Post-translational Modifications of the Protein Termini.Frontiers in cell and developmental biology · 2021
    Review
  18. International journal of molecular sciences · 2020
    Review
  19. Article
  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

12 authors at 7 institutions in 2 countries.

Fangliang Zhang1] University of Pennsylvania School of Veterinary Medicine, Philadelphia, Pennsylvania 19104, USA. [2] University of Miami School of Medicine, and Sylvester Comprehensive Cancer Center, Miami, Florida 33136, USA.
Devang M PatelUniversity of Miami School of Medicine, and Sylvester Comprehensive Cancer Center, Miami, Florida 33136, USA.
Kristen ColavitaUniversity of Pennsylvania School of Veterinary Medicine, Philadelphia, Pennsylvania 19104, USA.
Irina RodionovaSanford Burnham Medical Research Institute, La Jolla, California 92037, USA.
Brian BuckleyRoswell Park Cancer Institute, Buffalo, New York, 14263, USA.
David A ScottSanford Burnham Medical Research Institute, La Jolla, California 92037, USA.
Akhilesh KumarUniversity of Miami School of Medicine, and Sylvester Comprehensive Cancer Center, Miami, Florida 33136, USA.
Svetlana A ShabalinaNational Center for Biotechnology Information, NLM, NIH, Bethesda, Maryland 20894, USA.
Sougata Saha1] University of Pennsylvania School of Veterinary Medicine, Philadelphia, Pennsylvania 19104, USA. [2] Department of Molecular Biology and Biotechnology, Tezpur University, Napaam 784028, India.
Mikhail ChernovRoswell Park Cancer Institute, Buffalo, New York, 14263, USA.
Andrei L OstermanSanford Burnham Medical Research Institute, La Jolla, California 92037, USA.
Anna KashinaUniversity of Pennsylvania School of Veterinary Medicine, Philadelphia, Pennsylvania 19104, USA.
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of Pennsylvania · USRoswell Park Comprehensive Cancer Center · USNational Center for Biotechnology Information · USSylvester Comprehensive Cancer Center · USTezpur University · INUniversity of Miami · US

Funding

Regulation of cadherin-based cell adhesions by talin proteolysis and arginylationR01GM107333 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI ZHANG, FANGLIANG · 2013 to 2017
$1.5M
Regulation of actin during cell migrationR01GM108744 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KASHINA, ANNA S · 2014 to 2017
$1.4M
Molecular Mechanisms of Protein ArginylationR01GM104003 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KASHINA, ANNA S · 2013 to 2016
$1.3M
Intramural NIH HHSNIGMS NIH HHS GM104003NIGMS NIH HHS GM107333NIGMS NIH HHS GM117984NIGMS NIH HHS R01 GM104003NIGMS NIH HHS R01 GM107333NIGMS NIH HHS R01 GM108744
6 · The paper itself

Abstract

Protein arginylation is an emerging post-translational modification that targets a number of metabolic enzymes; however, the mechanisms and downstream effects of this modification are unknown. Here we show that lack of arginylation renders cells vulnerable to purine nucleotide synthesis inhibitors and affects the related glycine and serine biosynthesis pathways. We show that the purine nucleotide biosynthesis enzyme PRPS2 is selectively arginylated, unlike its close homologue PRPS1, and that arginylation of PRPS2 directly facilitates its biological activity. Moreover, selective arginylation of PRPS2 but not PRPS1 is regulated through a coding sequence-dependent mechanism that combines elements of mRNA secondary structure with lysine residues encoded near the N-terminus of PRPS1. This mechanism promotes arginylation-specific degradation of PRPS1 and selective retention of arginylated PRPS2 in vivo. We therefore demonstrate that arginylation affects both the activity and stability of a major metabolic enzyme.

Indexed as

AminoacyltransferasesAnimalsArginineBlotting, WesternCell LineGlycineHEK293 CellsHumansLysineMiceMice, KnockoutMolecular StructureProtein Processing, Post-TranslationalPurine NucleotidesReverse Transcriptase Polymerase Chain ReactionRibose-Phosphate PyrophosphokinaseAminoacyltransferasesArgininearginyltransferaseGlycineLysinePRPS1 protein, mousePRPS2 protein, mousePurine NucleotidesRibose-Phosphate PyrophosphokinaseRNA, MessengerSerine

Identifiers

PMID26175007
PMCPMC4503932
OpenAlexW2265594330

What OpenQuestion 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 OpenQuestion graph.