Structure of full-length human TRPM4
Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a close...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 115; no. 10; pp. 2377 - 2382 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
06.03.2018
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na⁺-bound, apo state at pH 7.5 to an overall resolution of 3.7 Å. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4–S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via π–π bonds and cation–π bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4. |
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| AbstractList | Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na
-bound, apo state at pH 7.5 to an overall resolution of 3.7 Å. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4-S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via π-π bonds and cation-π bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4. Significance Ion channels are proteins that mediate the flow of ions across cell membranes. Human genetic mutations of one type of ion channel, called hTRPM4, underlie a form of progressive familial heart block. Its distribution among many tissues, however, suggests that its functions are broad. We have solved the atomic structure of hTRPM4 to an overall resolution of 3.7 Å. The channel is composed of four identical subunits surrounding a central pore. We show the path of Na + ions through the channel and point out aspects of the channel’s internal machinery that may affect its function. The structure will enable more directed experiments to understand the physiological function of this channel. Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na + -bound, apo state at pH 7.5 to an overall resolution of 3.7 Å. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4–S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via π–π bonds and cation–π bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4. Ion channels are proteins that mediate the flow of ions across cell membranes. Human genetic mutations of one type of ion channel, called hTRPM4, underlie a form of progressive familial heart block. Its distribution among many tissues, however, suggests that its functions are broad. We have solved the atomic structure of hTRPM4 to an overall resolution of 3.7 Å. The channel is composed of four identical subunits surrounding a central pore. We show the path of Na + ions through the channel and point out aspects of the channel’s internal machinery that may affect its function. The structure will enable more directed experiments to understand the physiological function of this channel. Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na + -bound, apo state at pH 7.5 to an overall resolution of 3.7 Å. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4–S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via π–π bonds and cation–π bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4. Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na⁺-bound, apo state at pH 7.5 to an overall resolution of 3.7 Å. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4–S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via π–π bonds and cation–π bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4. Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na+-bound, apo state at pH 7.5 to an overall resolution of 3.7 A. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4-S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via π-π bonds and cation-π bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4. Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na+-bound, apo state at pH 7.5 to an overall resolution of 3.7 Å. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4-S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via π-π bonds and cation-π bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4. |
| Author | Santa-Cruz, Ana Li, Zongli Zhang, Jin Duan, Jingjing Sanchez-Martinez, Silvia Clapham, David E. Li, Jian |
| Author_xml | – sequence: 1 givenname: Jingjing surname: Duan fullname: Duan, Jingjing organization: Howard Hughes Medical Institute, Ashburn, VA 20147 – sequence: 2 givenname: Zongli surname: Li fullname: Li, Zongli organization: Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115 – sequence: 3 givenname: Jian surname: Li fullname: Li, Jian organization: School of Basic Medical Sciences, Nanchang University, Nanchang, 330031 Jiangxi, China – sequence: 4 givenname: Ana surname: Santa-Cruz fullname: Santa-Cruz, Ana organization: Howard Hughes Medical Institute, Ashburn, VA 20147 – sequence: 5 givenname: Silvia surname: Sanchez-Martinez fullname: Sanchez-Martinez, Silvia organization: Howard Hughes Medical Institute, Ashburn, VA 20147 – sequence: 6 givenname: Jin surname: Zhang fullname: Zhang, Jin organization: School of Basic Medical Sciences, Nanchang University, Nanchang, 330031 Jiangxi, China – sequence: 7 givenname: David E. surname: Clapham fullname: Clapham, David E. organization: Howard Hughes Medical Institute, Ashburn, VA 20147 |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29463718$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | Volumes 1–89 and 106–114, copyright as a collective work only; author(s) retains copyright to individual articles Copyright © 2018 the Author(s). Published by PNAS. Copyright National Academy of Sciences Mar 6, 2018 Copyright © 2018 the Author(s). Published by PNAS. 2018 |
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| DocumentTitleAlternate | Cryo-EM structure of human TRPM4 |
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| Issue | 10 |
| Keywords | cryomicroscopy cardiac arrhythmia ion channel transient receptor potential channel |
| Language | English |
| License | Copyright © 2018 the Author(s). Published by PNAS. This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND). |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Reviewers: M.T.N., University of Vermont; D.R., University of Pennsylvania; and T.V., VIB-KU Leuven Center for Brain & Disease Research. 1J.D., Z.L., and J.L. contributed equally to this work. Contributed by David E. Clapham, January 25, 2018 (sent for review December 19, 2017; reviewed by Mark T. Nelson, Dejian Ren, and Thomas Voets) Author contributions: J.D., Z.L., J.Z., and D.E.C. designed research; J.D., Z.L., J.L., A.S.-C., S.S.-M., and J.Z. performed research; Z.L., J.L., A.S.-C., S.S.-M., and J.Z. contributed new reagents/analytic tools; J.D., Z.L., J.L., A.S.-C., S.S.-M., J.Z., and D.E.C. analyzed data; and J.D., Z.L., A.S.-C., J.Z., and D.E.C. wrote the paper. |
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| Snippet | Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations... Significance Ion channels are proteins that mediate the flow of ions across cell membranes. Human genetic mutations of one type of ion channel, called hTRPM4,... Ion channels are proteins that mediate the flow of ions across cell membranes. Human genetic mutations of one type of ion channel, called hTRPM4, underlie a... |
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| SubjectTerms | Binding sites Biological Sciences Calcium Cations Channel gating Coils Conduction Genes Glycosylation Ions Lipids Mutation Sodium Transient receptor potential proteins |
| Title | Structure of full-length human TRPM4 |
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