Evidence map›Paper›PMID 40126401›Full record

ReviewPhysiology (Bethesda, Md.)2025

MFSD2A in Focus: the Molecular Mechanism of Omega-3 Fatty Acid Transport.

Farrah Blades, Aysenur Torun Yazici, Rosemary Jane Cater, Filippo Mancia

Abstract readReview
In one paragraph

Review in Physiology (Bethesda, Md.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. 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

4 authors.

Farrah BladesInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Queensland, Australia.
Aysenur Torun YaziciDepartment of Physiology and Cellular Biophysics, Columbia University, New York, New York, United States.
Rosemary Jane CaterInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Queensland, Australia.
Filippo ManciaDepartment of Physiology and Cellular Biophysics, Columbia University, New York, New York, United States.ORCID 0000-0003-3293-2200

Funding

Structural basis of receptor-mediated cellular vitamin A uptakeR01EY027405 · NEI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI George Khelashvili, Filippo Mancia · 2017 to 2026
$4.4M
Structural basis of integral membrane enzyme functionR35GM132120 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Filippo Mancia · 2019 to 2026
$3.7M
Molecular mechanism of omega-3 fatty acid transport into the brainR21MH125649 · NIMH · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MANCIA, FILIPPO · 2021 to 2022
$446k
Department of Education and Training | Australian Research Council (ARC) DE230101536HHS | NIH | National Eye Institute (NEI) R01EY027405HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35GM132120HHS | NIH | National Institute of Mental Health (NIMH) R21MH125649NEI NIH HHS R01 EY027405NIGMS NIH HHS R35 GM132120NIMH NIH HHS R21 MH125649
6 · The paper itself

Abstract

Omega-3 fatty acids, such as docosahexaenoic acid (DHA), are essential nutrients required to support the growth, maintenance, and function of the central nervous system (CNS). While the brain has a high demand for DHA, it cannot synthesize it de novo and thus relies on its uptake from the bloodstream. Circulating DHA is primarily obtained from dietary sources and is transported across the blood-brain barrier (BBB) in the form of lysophosphatidylcholine (LPC-DHA) by the transmembrane transporter major facilitator superfamily domain containing 2A (MFSD2A) in a sodium-dependent manner. Here we provide a comprehensive analysis of recent insights gained from structural, functional, and computational studies of MFSD2A. We focus on the mechanism by which this transporter mediates sodium-dependent uptake of LPC-DHA, and lysolipids more broadly, highlighting different conformational states, substrate entry and release pathways, and the ligand binding sites. This review presents a detailed overview of the molecular mechanism that enables MFSD2A to supply the brain with this essential nutrient, while simultaneously providing biophysical insights into how lysolipids are transported across biological membranes.

Indexed as

Fatty Acids, Omega-3SymportersAnimalsBiological TransportBlood-Brain BarrierBrainDocosahexaenoic AcidsHumansDocosahexaenoic AcidsFatty Acids, Omega-3MFSD2A protein, humanSymportersblood-brain barriercryo-EMdocosahexaenoic acidlysolipidMFS transporters

Identifiers

PMID40126401
PMCPMC12178809

What OpenQuestion holds

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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.