Evidence map›Paper›PMID 24981175›Full record

ArticleMolecular cell2014

Akt phosphorylation and regulation of transketolase is a nodal point for amino acid control of purine synthesis.

Arindam Saha, Stephen Connelly, Jingjing Jiang, Shunhui Zhuang, Deron T Amador, Tony Phan, Renate B Pilz, Gerry R Boss

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

68 citing papers in PubMed, 104 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. The PI3K/Akt Pathway and Glucose Metabolism: A Dangerous Liaison in Cancer.International journal of biological sciences · 2024
    Review

8 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

Arindam SahaDepartment of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Stephen ConnellyDepartment of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.
Jingjing JiangDepartment of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Shunhui ZhuangDepartment of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Deron T AmadorDepartment of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Tony PhanDepartment of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Renate B PilzDepartment of Medicine, University of California, San Diego, La Jolla, CA 92093, USA. Electronic address: rpilz@ucsd.edu.
Gerry R BossDepartment of Medicine, University of California, San Diego, La Jolla, CA 92093, USA. Electronic address: gboss@ucsd.edu.
University of California, San Diego · USScripps Research Institute · US

Funding

REGULATION OF GENE EXPRESSION BY cGMP and PKG IN BONER01AR051300 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PILZ, RENATE B · 2004 to 2014
$3.1M
NIAMS NIH HHS R01 AR051300NIAMS NIH HHS R01AR051300
6 · The paper itself

Abstract

The phosphatidylinositol 3-kinase (PI3K)/Akt pathway integrates environmental clues to regulate cell growth and survival. We showed previously that depriving cells of a single essential amino acid rapidly and reversibly arrests purine synthesis. Here we demonstrate that amino acids via mammalian target of rapamycin 2 and IκB kinase regulate Akt activity and Akt association and phosphorylation of transketolase (TKT), a key enzyme of the nonoxidative pentose phosphate pathway (PPP). Akt phosphorylates TKT on Thr382, markedly enhancing enzyme activity and increasing carbon flow through the nonoxidative PPP, thereby increasing purine synthesis. Mice fed a lysine-deficient diet for 2 days show decreased Akt activity, TKT activity, and purine synthesis in multiple organs. These results provide a mechanism whereby Akt coordinates amino acid availability with glucose utilization, purine synthesis, and RNA and DNA synthesis.

Indexed as

Protein Processing, Post-TranslationalAmino AcidsAmino Acid SequenceAnimalsConserved SequenceHeLa CellsHumansI-kappa B KinaseMaleMechanistic Target of Rapamycin Complex 2MiceMice, Inbred C57BLMolecular Sequence DataMultiprotein ComplexesOxidation-ReductionPhosphoribosyl PyrophosphateAKT1 protein, humanAmino AcidsI-kappa B KinaseMechanistic Target of Rapamycin Complex 2Multiprotein ComplexesPhosphoribosyl PyrophosphateProto-Oncogene Proteins c-aktPurinesTOR Serine-Threonine KinasesTransketolase

Identifiers

PMID24981175
PMCPMC4104231
OpenAlexW1970519691

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.