Evidence map›Paper›PMID 21908621›Full record

ArticleThe Journal of biological chemistry2011

MondoA senses non-glucose sugars: regulation of thioredoxin-interacting protein (TXNIP) and the hexose transport curb.

Carrie A Stoltzman, Mohan R Kaadige, Christopher W Peterson, Donald E Ayer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

45 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mondo family proteins in diabetes.Frontiers in endocrinology · 2025
    Review
  5. Article
  6. Domestication GeneInternational journal of molecular sciences · 2024
    Article
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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

4 authors at 1 institution in 1 country.

Carrie A StoltzmanDepartment of Oncological Sciences and the Huntsman Cancer Institute, University of Utah, Salt Lake City, Utah 84112.
Mohan R KaadigeDepartment of Oncological Sciences and the Huntsman Cancer Institute, University of Utah, Salt Lake City, Utah 84112.
Christopher W PetersonDepartment of Oncological Sciences and the Huntsman Cancer Institute, University of Utah, Salt Lake City, Utah 84112.
Donald E AyerDepartment of Oncological Sciences and the Huntsman Cancer Institute, University of Utah, Salt Lake City, Utah 84112. Electronic address: don.ayer@hci.utah.edu.
University of Utah · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
Nutrient Sensing and Growth ControlR01GM055668 · NIGMS · UNIVERSITY OF UTAH · PI AYER, DONALD E · 1997 to 2015
$4.3M
CASEIN KINASE I AND THE REGULATION OF CIRCADIAN RHYTHMR01GM060387 · NIGMS · UNIVERSITY OF UTAH · PI AYER, DONALD E · 2002 to 2010
$2.4M
NCI NIH HHS 2P30CA42014NCI NIH HHS P30 CA042014NIGMS NIH HHS GM55668NIGMS NIH HHS GM60387NIGMS NIH HHS R01 GM055668NIGMS NIH HHS R01 GM060387
6 · The paper itself

Abstract

Glucose is required for cell growth and proliferation. The MondoA·Mlx transcription factor is glucose-responsive and accumulates in the nucleus by sensing glucose 6-phosphate. One direct and glucose-induced target of MondoA·Mlx complexes is thioredoxin-interacting protein (TXNIP). TXNIP is a potent negative regulator of glucose uptake, and hence its regulation by MondoA·Mlx triggers a feedback loop that restricts glucose uptake. This feedback loop is similar to the "hexose transport curb" first described almost 30 years ago. We show here that MondoA responds to the non-glucose hexoses, allose, 3-O-methylglucose, and glucosamine by accumulating in the nucleus and activating TXNIP transcription. The metabolic inhibitor 3-bromopyruvate blocks the transcriptional response to allose and 3-O-methylglucose, indicating that their metabolism, or a parallel pathway, is required to stimulate MondoA activity. Our dissection of the hexosamine biosynthetic pathway suggests that in addition to sensing glucose 6-phosphate, MondoA can also sense glucosamine 6-phosphate. Analysis of glucose uptake in wild-type, MondoA-null, or TXNIP-null murine embryonic fibroblasts indicates a role for the MondoA-TXNIP regulatory circuit in the hexose transport curb, although other redundant pathways also contribute.

Indexed as

2,4-Dinitrophenol3-O-MethylglucoseAnimalsBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCarrier ProteinsCell LineGlucoseGlucose-6-PhosphateHexosesHumansMiceMice, TransgenicPhosphorylationThioredoxinsTranscription, Genetic2,4-Dinitrophenol3-O-MethylglucosealloseBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCarrier ProteinsGlucoseGlucose-6-PhosphateHexosesMLXIP protein, humanMondoA protein, mouseThioredoxinsTXNIP protein, humanTxnip protein, mouse

Identifiers

PMID21908621
PMCPMC3207397
OpenAlexW2045679421

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.