Evidence map›Paper›PMID 42370679›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2026

Structure, assembly, and mechanism of the MmpL family of transporters.

Zhemin Zhang, Emma Kundracik, Wei Li, Svitlana Babii, Komal Choukate, Alex Aboagye, Philip A Klenotic, Rakesh Maharjan, William D Gregor, Benjamin M Swarts and 3 more

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Zhemin ZhangDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Emma KundracikDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Wei LiMycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA.
Svitlana BabiiDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma, USA.
Komal ChoukateDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma, USA.
Alex AboagyeDepartment of Chemistry and Biochemistry, Central Michigan University, Mount Pleasant, Michigan, USA.
Philip A KlenoticDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Rakesh MaharjanDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
William D GregorDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Benjamin M SwartsDepartment of Chemistry and Biochemistry, Central Michigan University, Mount Pleasant, Michigan, USA.
Helen I ZgurskayaDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma, USA.ORCID 0000-0001-8929-4727
Mary JacksonMycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA.ORCID 0000-0002-9212-0258
Edward W YuDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.ORCID 0000-0001-5912-1227

Funding

MmpL3 as a target for novel anti-TB agentsR01AI116525 · NIAID · COLORADO STATE UNIVERSITY · PI JACKSON, MARY · 2015 to 2024
$5.3M
Intermembrane transport of lipids and metabolites by mycobacterial MmpL protein complexesR01AI187294 · NIAID · UNIVERSITY OF OKLAHOMA · PI Mary Jackson, EDWARD W YU · 2025 to 2026
$1.6M
NIAID NIH HHS R01 AI116525NIAID NIH HHS R01 AI187294NIH HHS R01AI116525NIH HHS R01AI187294
6 · The paper itself

Abstract

SUMMARYThe mycobacterial cell envelope, one of the most complex membranes found in bacteria, plays a major role in bacterial pathogenesis, virulence, and antimicrobial resistance. Biogenesis and modeling of this cell envelope are heavily influenced by the mycobacterial membrane protein large (MmpL) family of transporters due to their ability to export fatty acids and lipid components. Select MmpL transporters can also function as siderophore exporters to help regulate the acquisition of iron, which is critical for mycobacterial survival. Additionally, certain MmpLs can participate in active efflux of antimycobacterial drugs, directly contributing to antimicrobial resistance. Given the physiological significance of these MmpL membrane proteins and their potential to serve as important antimycobacterial targets, questions regarding their functional roles, cellular assemblies, interactions, and regulation need to be fully addressed. In this review, we summarize our current knowledge on the structures and functions of these MmpL transporters. It is our hope that researchers in the field will continue to build upon these efforts and apply various structural, biophysical, and biochemical methodologies to fully elucidate how MmpL transporters coordinate to participate in cell envelope biogenesis, cell elongation and division, and antimicrobial resistance.

Indexed as

Bacterial ProteinsMembrane Transport ProteinsMycobacteriumBiological TransportCell MembraneCell WallIronBacterial ProteinsIronMembrane Transport Proteinscell envelopemembrane biogenesisMmpL3MmpL4MmpL5mycobacterial membrane protein large (MmpL)Mycobacterium

Identifiers

PMID42370679
PMCPMC13602945

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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.