Evidence map›Paper›PMID 36611873›Full record

ArticleCells2022

Glutamine Produces Ammonium to Tune Lysosomal pH and Regulate Lysosomal Function.

Jian Xiong, Thi Thu Trang Luu, Kartik Venkatachalam, Guangwei Du, Michael X Zhu

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Glutaminolysis is a Potential Therapeutic Target for Kidney Diseases.Diabetes, metabolic syndrome and obesity : targets and therapy · 2024
    Review
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

5 authors at 1 institution in 1 country.

Jian XiongDepartment of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
Thi Thu Trang LuuDepartment of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
Kartik VenkatachalamDepartment of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.ORCID 0000-0002-3055-9265
Guangwei DuDepartment of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
Michael X ZhuDepartment of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX 77030, USA.ORCID 0000-0002-5676-841X
The University of Texas MD Anderson Cancer Center · US

Funding

Neuropathology in tauopathies stem from depolarization-induced alterations in the planar distribution of phosphoinositidesRF1AG069076 · NIA · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI VENKATACHALAM, KARTIK · 2020 to 2020
$1.8M
A critical role for PLD1 in osteoclast fusionR01AR075830 · NIAMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DU, GUANGWEI · 2019 to 2023
$1.7M
Training Interdisciplinary Pharmacology Scientists (TIPS)T32GM139801 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI Carmen W. Dessauer · 2021 to 2026
$1.5M
Alterations in somatodendritic bioenergetics in Drosophila models of tauopathyRF1AG072176 · NIA · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI VENKATACHALAM, KARTIK · 2021 to 2021
$1.2M
Alterations in somatodendritic bioenergetics in Drosophila models of tauopathyR01AG072176 · NIA · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI KARTIK VENKATACHALAM · 2025 to 2026
$766k
Regulatory mechanisms of lysosomal degradation in neurodegenerative diseaseR21NS125167 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI ZHU, MICHAEL X · 2021 to 2021
$429k
NIAMS NIH HHS R01 AR075830NIA NIH HHS R01 AG072176NIA NIH HHS RF1 AG069076NIA NIH HHS RF1 AG072176NIGMS NIH HHS T32 GM139801NIH HHS NS102452, NS125167, AR075830, AG069076NINDS NIH HHS R21 NS125167
6 · The paper itself

Abstract

Glutamine is one of the most abundant amino acids in the cell. In mitochondria, glutaminases 1 and 2 (GLS1/2) hydrolyze glutamine to glutamate, which serves as the precursor of multiple metabolites. Here, we show that ammonium generated during GLS1/2-mediated glutaminolysis regulates lysosomal pH and in turn lysosomal degradation. In primary human skin fibroblasts BJ cells and mouse embryonic fibroblasts, deprivation of total amino acids for 1 h increased lysosomal degradation capacity as shown by the increased turnover of lipidated microtubule-associated proteins 1A/1B light chain 3B (LC3-II), several autophagic receptors, and endocytosed DQ-BSA. Removal of glutamine but not any other amino acids from the culture medium enhanced lysosomal degradation similarly as total amino acid starvation. The presence of glutamine in regular culture media increased lysosomal pH by >0.5 pH unit and the removal of glutamine caused lysosomal acidification. GLS1/2 knockdown, GLS1 antagonist, or ammonium scavengers reduced lysosomal pH in the presence of glutamine. The addition of glutamine or NH

Indexed as

Ammonium CompoundsGlutamineAmino AcidsAnimalsFibroblastsGlutamic AcidHumansHydrogen-Ion ConcentrationLysosomesMechanistic Target of Rapamycin Complex 1MiceAmino AcidsAmmonium CompoundsGlutamic AcidGlutamineMechanistic Target of Rapamycin Complex 1amino acid starvationautophagosomeautophagyglutaminaseglutaminelysosomal pHmTORC1 activation

Identifiers

PMID36611873
PMCPMC9819001
OpenAlexW4313246821

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.