Evidence map›Paper›PMID 38294434›Full record

ArticleThe Journal of general physiology2024

Transport of metformin metabolites by guanidinium exporters of the small multidrug resistance family.

Rachael M Lucero, Kemal Demirer, Trevor Justin Yeh, Randy B Stockbridge

Abstract read
In one paragraph

Article in The Journal of general physiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Peripheral positions encode transport specificity in the small multidrug resistance exporters.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. SMR transporters meet the challenge of metformin metabolites.The Journal of general physiology · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Rachael M LuceroProgram in Chemical Biology, University of Michigan, Ann Arbor, MI, USA.ORCID 0009-0004-7933-4683
Kemal DemirerDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.ORCID 0009-0000-4576-6526
Trevor Justin YehProgram in Biophysics, University of Michigan, Ann Arbor, MI, USA.ORCID 0000-0003-3749-641X
Randy B StockbridgeProgram in Chemical Biology, University of Michigan, Ann Arbor, MI, USA.ORCID 0000-0001-8848-3032

Funding

Structural and functional analysis of novel microbial membrane proteinsR35GM128768 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Randy B. Stockbridge · 2018 to 2026
$3.7M
NIGMS NIH HHS R35 GM128768NIH HHS R35-GM128768
6 · The paper itself

Abstract

Proteins from the small multidrug resistance (SMR) family are frequently associated with horizontally transferred multidrug resistance gene arrays found in bacteria from wastewater and the human-adjacent biosphere. Recent studies suggest that a subset of SMR transporters might participate in the metabolism of the common pharmaceutical metformin by bacterial consortia. Here, we show that both genomic and plasmid-associated transporters of the SMRGdx functional subtype export byproducts of microbial metformin metabolism, with particularly high export efficiency for guanylurea. We use solid-supported membrane electrophysiology to evaluate the transport kinetics for guanylurea and native substrate guanidinium by four representative SMRGdx homologs. Using an internal reference to normalize independent electrophysiology experiments, we show that transport rates are comparable for genomic and plasmid-associated SMRGdx homologs, and using a proteoliposome-based transport assay, we show that 2 proton:1 substrate transport stoichiometry is maintained. Additional characterization of guanidinium and guanylurea export properties focuses on the structurally characterized homolog, Gdx-Clo, for which we examined the pH dependence and thermodynamics of substrate binding and solved an x-ray crystal structure with guanylurea bound. Together, these experiments contribute in two main ways. By providing the first detailed kinetic examination of the structurally characterized SMRGdx homolog Gdx-Clo, they provide a functional framework that will inform future mechanistic studies of this model transport protein. Second, this study casts light on a potential role for SMRGdx transporters in microbial handling of metformin and its microbial metabolic byproducts, providing insight into how native transport physiologies are co-opted to contend with new selective pressures.

Indexed as

Membrane Transport ProteinsMetforminGuanidineHumansKineticsUreaGuanidineguanidine carboxamideMembrane Transport ProteinsMetforminUrea

Identifiers

PMID38294434
PMCPMC10829512

What Socratic 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 Socratic graph.