Structure and mechanism of blood–brain-barrier lipid transporter MFSD2A

MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain 1 , 2 , which is crucial for the development and performance of the brain 3 . Mutations that affect MFSD2A cause microcephaly syndromes 4 , 5 . The ability of MFSD...

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Published inNature (London) Vol. 596; no. 7872; pp. 444 - 448
Main Authors Wood, Chase A. P., Zhang, Jinru, Aydin, Deniz, Xu, Yan, Andreone, Benjamin J., Langen, Urs H., Dror, Ron O., Gu, Chenghua, Feng, Liang
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 19.08.2021
Nature Publishing Group
Subjects
101/28
631/378/1341
631/535/1258/1259
631/92/577
82
82/16
82/80
82/83
Animals
Binding Sites
Biological Transport
Blood-brain barrier
Blood-Brain Barrier - metabolism
Carrier proteins
Disorders
Docosahexaenoic acid
Drug delivery
Dynamic structural analysis
Electron microscopy
Health aspects
HEK293 Cells
Humanities and Social Sciences
Humans
Lipid Metabolism
Lipids
Lysophosphatidylcholine
Membrane permeability
Mice
Microcephaly
Microscopy
Models, Molecular
Modulators
Molecular dynamics
Molecular Dynamics Simulation
multidisciplinary
Mutagenesis
Mutation
Permeability
Physiological aspects
Protein Domains
Science
Science (multidisciplinary)
Simulation
Sodium
Sodium - metabolism
Structure
Substrates
Symporters - chemistry
Symporters - genetics
Symporters - metabolism
Symporters - ultrastructure
Therapeutic applications
United States
Online AccessGet full text

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Abstract MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain 1 , 2 , which is crucial for the development and performance of the brain 3 . Mutations that affect MFSD2A cause microcephaly syndromes 4 , 5 . The ability of MFSD2A to transport lipid is also a key mechanism that underlies its function as an inhibitor of transcytosis to regulate the blood–brain barrier 6 , 7 . Thus, MFSD2A represents an attractive target for modulating the permeability of the blood–brain barrier for drug delivery. Here we report the cryo-electron microscopy structure of mouse MFSD2A. Our structure defines the architecture of this important transporter, reveals its unique extracellular domain and uncovers its substrate-binding cavity. The structure—together with our functional studies and molecular dynamics simulations—identifies a conserved sodium-binding site, reveals a potential lipid entry pathway and helps to rationalize MFSD2A mutations that underlie microcephaly syndromes. These results shed light on the critical lipid transport function of MFSD2A and provide a framework to aid in the design of specific modulators for therapeutic purposes. The cryo-electron microscopy structure of mouse MFSD2A sheds light on the mechanism that underlies its lipid transport functions, which have a pivotal role in regulating the blood–brain barrier.
AbstractList MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain, which is crucial for the development and performance of the brain. Mutations that affect MFSD2A cause microcephaly syndromes. The ability of MFSD2A to transport lipid is also a key mechanism that underlies its function as an inhibitor of transcytosis to regulate the blood-brain barrier. Thus, MFSD2A represents an attractive target for modulating the permeability of the blood-brain barrier for drug delivery. Here we report the cryo-electron microscopy structure of mouse MFSD2A. Our structure defines the architecture of this important transporter, reveals its unique extracellular domain and uncovers its substrate-binding cavity. The structure-together with our functional studies and molecular dynamics simulations-identifies a conserved sodium-binding site, reveals a potential lipid entry pathway and helps to rationalize MFSD2A mutations that underlie microcephaly syndromes. These results shed light on the critical lipid transport function of MFSD2A and provide a framework to aid in the design of specific modulators for therapeutic purposes.
MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain.sup.1,2, which is crucial for the development and performance of the brain.sup.3. Mutations that affect MFSD2A cause microcephaly syndromes.sup.4,5. The ability of MFSD2A to transport lipid is also a key mechanism that underlies its function as an inhibitor of transcytosis to regulate the blood-brain barrier.sup.6,7. Thus, MFSD2A represents an attractive target for modulating the permeability of the blood-brain barrier for drug delivery. Here we report the cryo-electron microscopy structure of mouse MFSD2A. Our structure defines the architecture of this important transporter, reveals its unique extracellular domain and uncovers its substrate-binding cavity. The structure--together with our functional studies and molecular dynamics simulations--identifies a conserved sodium-binding site, reveals a potential lipid entry pathway and helps to rationalize MFSD2A mutations that underlie microcephaly syndromes. These results shed light on the critical lipid transport function of MFSD2A and provide a framework to aid in the design of specific modulators for therapeutic purposes.
MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain 1 , 2 , which is crucial for the development and performance of the brain 3 . Mutations that affect MFSD2A cause microcephaly syndromes 4 , 5 . The ability of MFSD2A to transport lipid is also a key mechanism that underlies its function as an inhibitor of transcytosis to regulate the blood–brain barrier 6 , 7 . Thus, MFSD2A represents an attractive target for modulating the permeability of the blood–brain barrier for drug delivery. Here we report the cryo-electron microscopy structure of mouse MFSD2A. Our structure defines the architecture of this important transporter, reveals its unique extracellular domain and uncovers its substrate-binding cavity. The structure—together with our functional studies and molecular dynamics simulations—identifies a conserved sodium-binding site, reveals a potential lipid entry pathway and helps to rationalize MFSD2A mutations that underlie microcephaly syndromes. These results shed light on the critical lipid transport function of MFSD2A and provide a framework to aid in the design of specific modulators for therapeutic purposes. The cryo-electron microscopy structure of mouse MFSD2A sheds light on the mechanism that underlies its lipid transport functions, which have a pivotal role in regulating the blood–brain barrier.
MFSD2A is a sodium-dependent lysophosphatidylcholine (LPC) symporter responsible for docosahexaenoic acid (DHA) uptake into the brain 1 , 2 , which is crucial for brain development and performance 3 . Its mutations cause microcephaly syndromes 4 , 5 . MFSD2A’s ability to transport lipid is also a key mechanism underlying its function as a transcytosis inhibitor to regulate the blood-brain barrier (BBB) 6 , 7 . Thus, MFSD2A represents an attractive target for modulating BBB permeability for drug delivery. Herein, we report the cryo-electron microscopy structure of MFSD2A. Our structure defines this important transporter's architecture, reveals its unique extracellular domain, and uncovers the substrate-binding cavity. The structure, together with our functional studies and molecular dynamics simulations, identifies a conserved sodium-binding site, reveals a potential lipid entry pathway, and helps rationalize MFSD2A mutations that underlie microcephaly syndromes. These results shed light on MFSD2A's critical lipid transport function and lay a framework to aid the design of specific modulators for therapeutic purposes.
MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain , which is crucial for the development and performance of the brain . Mutations that affect MFSD2A cause microcephaly syndromes . The ability of MFSD2A to transport lipid is also a key mechanism that underlies its function as an inhibitor of transcytosis to regulate the blood-brain barrier . Thus, MFSD2A represents an attractive target for modulating the permeability of the blood-brain barrier for drug delivery. Here we report the cryo-electron microscopy structure of mouse MFSD2A. Our structure defines the architecture of this important transporter, reveals its unique extracellular domain and uncovers its substrate-binding cavity. The structure-together with our functional studies and molecular dynamics simulations-identifies a conserved sodium-binding site, reveals a potential lipid entry pathway and helps to rationalize MFSD2A mutations that underlie microcephaly syndromes. These results shed light on the critical lipid transport function of MFSD2A and provide a framework to aid in the design of specific modulators for therapeutic purposes.
MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain.sup.1,2, which is crucial for the development and performance of the brain.sup.3. Mutations that affect MFSD2A cause microcephaly syndromes.sup.4,5. The ability of MFSD2A to transport lipid is also a key mechanism that underlies its function as an inhibitor of transcytosis to regulate the blood-brain barrier.sup.6,7. Thus, MFSD2A represents an attractive target for modulating the permeability of the blood-brain barrier for drug delivery. Here we report the cryo-electron microscopy structure of mouse MFSD2A. Our structure defines the architecture of this important transporter, reveals its unique extracellular domain and uncovers its substrate-binding cavity. The structure--together with our functional studies and molecular dynamics simulations--identifies a conserved sodium-binding site, reveals a potential lipid entry pathway and helps to rationalize MFSD2A mutations that underlie microcephaly syndromes. These results shed light on the critical lipid transport function of MFSD2A and provide a framework to aid in the design of specific modulators for therapeutic purposes. The cryo-electron microscopy structure of mouse MFSD2A sheds light on the mechanism that underlies its lipid transport functions, which have a pivotal role in regulating the blood-brain barrier.
Audience Academic
Author Zhang, Jinru
Andreone, Benjamin J.
Feng, Liang
Xu, Yan
Langen, Urs H.
Dror, Ron O.
Wood, Chase A. P.
Aydin, Deniz
Gu, Chenghua
AuthorAffiliation 4 Institute for Computational and Mathematical Engineering, Stanford University, Stanford, CA 94305, USA
3 Department of Computer Science, Stanford University, Stanford, CA 94305, USA
2 Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA
5 Department of Neurobiology, Harvard Medical School, 220 Longwood Avenue, Boston, MA 02115, USA
1 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/34349262$$D View this record in MEDLINE/PubMed
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License 2021. The Author(s), under exclusive licence to Springer Nature Limited.
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content type line 23
These authors contributed equally.
Author contributions. C.A.P.W. and J.Z. carried out biochemical, functional and cryo-EM studies. D.A. carried out and analyzed MD simulations under the guidance of R.O.D. Y.X. assisted with functional and biochemical studies. B.A. and U.H.L. characterized the scFv. C.G. supervised the generation and characterizations of scFv. L.F. directed biochemical, functional and structural studies. C.A.P.W., J.Z. and L.F. wrote the manuscript with input from all authors.
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SSID ssj0005174
Score 2.5818594
Snippet MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain 1 , 2 , which is...
MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain , which is crucial for...
MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain.sup.1,2, which is...
MFSD2A is a sodium-dependent lysophosphatidylcholine symporter that is responsible for the uptake of docosahexaenoic acid into the brain, which is crucial for...
MFSD2A is a sodium-dependent lysophosphatidylcholine (LPC) symporter responsible for docosahexaenoic acid (DHA) uptake into the brain 1 , 2 , which is crucial...
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SubjectTerms 101/28
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Animals
Binding Sites
Biological Transport
Blood-brain barrier
Blood-Brain Barrier - metabolism
Carrier proteins
Disorders
Docosahexaenoic acid
Drug delivery
Dynamic structural analysis
Electron microscopy
Health aspects
HEK293 Cells
Humanities and Social Sciences
Humans
Lipid Metabolism
Lipids
Lysophosphatidylcholine
Membrane permeability
Mice
Microcephaly
Microscopy
Models, Molecular
Modulators
Molecular dynamics
Molecular Dynamics Simulation
multidisciplinary
Mutagenesis
Mutation
Permeability
Physiological aspects
Protein Domains
Science
Science (multidisciplinary)
Simulation
Sodium
Sodium - metabolism
Structure
Substrates
Symporters - chemistry
Symporters - genetics
Symporters - metabolism
Symporters - ultrastructure
Therapeutic applications
Title Structure and mechanism of blood–brain-barrier lipid transporter MFSD2A
URI https://link.springer.com/article/10.1038/s41586-021-03782-y
https://www.ncbi.nlm.nih.gov/pubmed/34349262
https://www.proquest.com/docview/2563511324
https://search.proquest.com/docview/2558450160
https://pubmed.ncbi.nlm.nih.gov/PMC8884080
Volume 596
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