Evidence map›Paper›PMID 31337707›Full record

ArticleThe Journal of biological chemistry2019

ANKRD9 is a metabolically-controlled regulator of IMPDH2 abundance and macro-assembly.

Dawn Hayward, Valentina L Kouznetsova, Hannah E Pierson, Nesrin M Hasan, Estefany R Guzman, Igor F Tsigelny, Svetlana Lutsenko

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. A journey into the regulatory secrets of theFrontiers in pharmacology · 2024
    Review
  11. Article
  12. Article
  13. The gateway to guanine nucleotides: Allosteric regulation of IMP dehydrogenases.Protein science : a publication of the Protein Society · 2022
    Review
  14. Observational
  15. Article
  16. Article
  17. Review
  18. Freedom of assembly: metabolic enzymes come together.Molecular biology of the cell · 2020
    Article
  19. 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

7 authors at 2 institutions in 1 country.

Dawn HaywardDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Valentina L KouznetsovaThe Moores Cancer Center, University of California San Diego, La Jolla, California 92093.
Hannah E PiersonDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Nesrin M HasanDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Estefany R GuzmanDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Igor F TsigelnyDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Svetlana LutsenkoDepartment of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 Lutsenko@jhmi.edu.ORCID 0000-0001-5275-2587
Johns Hopkins University · USSan Diego Supercomputer Center · US

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
Molecular Mechanisms of ATP-dependent Copper TransportersR01DK071865 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI SVETLANA LUTSENKO · 2005 to 2026
$7.9M
Molecular Mechanisms of ATP-Dependent Copper TransportersR56DK071865 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI LUTSENKO, SVETLANA · 2018 to 2018
$539k
Olympus FluoView3000RS Confocal MicroscopeS10OD025244 · OD · JOHNS HOPKINS UNIVERSITY · PI O'ROURKE, BRIAN · 2018 to 2018
$448k
NIDDK NIH HHS R01 DK071865NIDDK NIH HHS R56 DK071865NIGMS NIH HHS T32 GM007445NIH HHS S10 OD025244
6 · The paper itself

Abstract

Members of a large family of Ankyrin Repeat Domain (ANKRD) proteins regulate numerous cellular processes by binding to specific protein targets and modulating their activity, stability, and other properties. The same ANKRD protein may interact with different targets and regulate distinct cellular pathways. The mechanisms responsible for switches in the ANKRDs' behavior are often unknown. We show that cells' metabolic state can markedly alter interactions of an ANKRD protein with its target and the functional outcomes of this interaction. ANKRD9 facilitates degradation of inosine monophosphate dehydrogenase 2 (IMPDH2), the rate-limiting enzyme in GTP biosynthesis. Under basal conditions ANKRD9 is largely segregated from the cytosolic IMPDH2 in vesicle-like structures. Upon nutrient limitation, ANKRD9 loses its vesicular pattern and assembles with IMPDH2 into rodlike filaments, in which IMPDH2 is stable. Inhibition of IMPDH2 activity with ribavirin favors ANKRD9 binding to IMPDH2 rods. The formation of ANKRD9/IMPDH2 rods is reversed by guanosine, which restores ANKRD9 associations with the vesicle-like structures. The conserved Cys

Indexed as

Binding SitesCytoplasmic VesiclesGuanosineHEK293 CellsHeLa CellsHumansIMP DehydrogenaseIntracellular Signaling Peptides and ProteinsNutrientsProtein BindingProtein MultimerizationProtein StabilityTumor Suppressor ProteinsANKRD9 protein, humanGuanosineIMP DehydrogenaseIMPDH2 protein, humanIntracellular Signaling Peptides and ProteinsNutrientsTumor Suppressor ProteinsANKRD9ankyrinankyrin repeat domaincell metabolismcomplexcytoophidiaGTPIMPDH2nucleotideprotein-protein interactionrod

Identifiers

PMID31337707
PMCPMC6768640
OpenAlexW2962903893

What OpenQuestion holds

Textmetadata
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.