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Keywords {🔍}

lipid, fig, groove, scrambling, article, pubmed, nhtmem, scholar, google, lipids, cas, residues, supplementary, extracellular, membrane, figure, nature, pathway, ion, channel, simulations, central, data, protein, liposomes, tmem, translocation, interactions, time, proteins, rate, side, activity, presence, ads, mechanism, absence, fold, interaction, headgroups, mutations, scramblase, leaflet, transport, network, opening, phospholipid, mutant, chem, molecular,

Topics {✒️}

nature portfolio }}\mathop {\rightleftarrows}\limits_\beta^\alpha l_{\mathrm{ c-terminal myc-streptavidin-binding peptide privacy policy national research foundation amino]hexanoyl}-sn-glycero-3-phosphoethanolamine 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho advertising shaw research 2% n-dodecyl-β-d-maltopyranoside n-octyl-β-d-glucopyranoside social media author information authors reprints dynamic nature semi-isotropic pressure coupling special-purpose supercomputer machine54 charge-reversed mutant e313r/r432e development calcium-dependent phospholipid scrambling long-lived inactivated state tmem16a/16f chimeras entails nature 497 nature 468 nature 516 nature 552 nature 455 nature bio-beads sm-2 adsorbent original author multi-scale iterative protocol tmem16f-independent pathways contribute charmm36 force-field parameters single mono-disperse peaks charmm-gui web-server50 charmm-gui martini maker mechanisms regulating access protein-coupled receptor opsin37 protein-coupled receptor opsin ca2+-activated cl− channels typically 5 μg protein/mg nose-hoover langevin piston53 ca2+-activated phospholipid scramblases gfp-based optimization scheme ca2+-dependent phospholipid scramblases total cl− content dys-regulated phosphatidylserine externalization $$f_{\mathrm{tot}}\left f_{\mathrm{scr}}\left

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      headline:Gating mechanism of the extracellular entry to the lipid pathway in a TMEM16 scramblase
      description:Members of the TMEM16/ANO family of membrane proteins are Ca2+-activated phospholipid scramblases and/or Cl− channels. A membrane-exposed hydrophilic groove in these proteins serves as a shared translocation pathway for ions and lipids. However, the mechanism by which lipids gain access to and permeate through the groove remains poorly understood. Here, we combine quantitative scrambling assays and molecular dynamic simulations to identify the key steps regulating lipid movement through the groove. Lipid scrambling is limited by two constrictions defined by evolutionarily conserved charged and polar residues, one extracellular and the other near the membrane mid-point. The region between these constrictions is inaccessible to lipids and water molecules, suggesting that the groove is in a non-conductive conformation. A sequence of lipid-triggered reorganizations of interactions between these residues and the permeating lipids propagates from the extracellular entryway to the central constriction, allowing the groove to open and coordinate the headgroups of transiting lipids. Some TMEM16 family members are Ca2+-dependent phospholipid scramblases, which also mediate non-selective ion transport; however, the mechanism how lipids permeate through the TMEM16 remains poorly understood. Here, the authors combine biochemical assays and simulations to identify the key steps regulating lipid movement through the membrane-exposed groove.
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