Recent progress in structural studies on TMEM16A channel
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Barish, 1983, A transient calcium-dependent chloride current in the immature Xenopus oocyte, J Physiol, 342, 309, 10.1113/jphysiol.1983.sp014852
Miledi, 1982, A calcium-dependent transient outward current in Xenopus laevis oocytes, Proc R Soc Lond B Biol Sci, 215, 491, 10.1098/rspb.1982.0056
Huang, 2009, Studies on expression and function of the TMEM16A calcium-activated chloride channel, Proc Natl Acad Sci U S A, 106, 21413, 10.1073/pnas.0911935106
Oh, 2016, Cellular functions of TMEM16/anoctamin, Pflugers Arch, 468, 443, 10.1007/s00424-016-1790-0
Caputo, 2008, TMEM16A, a membrane protein associated with calcium-dependent chloride channel activity, Science, 322, 590, 10.1126/science.1163518
Schroeder, 2008, Expression cloning of TMEM16A as a calcium-activated chloride channel subunit, Cell, 134, 1019, 10.1016/j.cell.2008.09.003
Yang, 2008, TMEM16A confers receptor-activated calcium-dependent chloride conductance, Nature, 455, 1210, 10.1038/nature07313
Pifferi, 2009, TMEM16B induces chloride currents activated by calcium in mammalian cells, Pflügers Arch Eur J Physiol, 458, 1023, 10.1007/s00424-009-0684-9
Gyobu, 2016, A role of TMEM16E carrying a scrambling domain in sperm motility, Mol Cell Biol, 36, 645, 10.1128/MCB.00919-15
Suzuki, 2013, Calcium-dependent phospholipid scramblase activity of TMEM16 protein family members, J Biol Chem, 288, 13305, 10.1074/jbc.M113.457937
Suzuki, 2010, Calcium-dependent phospholipid scrambling by TMEM16F, Nature, 468, 834, 10.1038/nature09583
Tian, 2012, Anoctamins are a family of Ca2+-activated Cl-channels, J Cell Sci, 125, 4991
Brunner, 2014, X-ray structure of a calcium-activated TMEM16 lipid scramblase, Nature, 516, 207, 10.1038/nature13984
Malvezzi, 2013, Ca2+-dependent phospholipid scrambling by a reconstituted TMEM16 ion channel, Nat Commun, 4, 2367, 10.1038/ncomms3367
Contreras-Vite, 2016, Revealing the activation pathway for TMEM16A chloride channels from macroscopic currents and kinetic models, Pflugers Arch, 468, 1241, 10.1007/s00424-016-1830-9
Cruz-Rangel, 2015, Gating modes of calcium-activated chloride channels TMEM16A and TMEM16B, J Physiol, 593, 5283, 10.1113/JP271256
Terashima, 2013, Purified TMEM16A is sufficient to form Ca2+-activated Cl-channels, Proc Natl Acad Sci U S A, 110, 19354, 10.1073/pnas.1312014110
Xiao, 2011, Voltage- and calcium-dependent gating of TMEM16A/Ano1 chloride channels are physically coupled by the first intracellular loop, Proc Natl Acad Sci U S A, 108, 8891, 10.1073/pnas.1102147108
Le, 2019, Molecular basis of PIP2-dependent regulation of the Ca(2+)-activated chloride channel TMEM16A, Nat Commun, 10, 3769, 10.1038/s41467-019-11784-8
Yu, 2019, A network of phosphatidylinositol 4,5-bisphosphate binding sites regulates gating of the Ca(2+)-activated Cl(-) channel ANO1 (TMEM16A), Proc Natl Acad Sci U S A, 116, 19952, 10.1073/pnas.1904012116
De Jesus-Perez, 2018, Phosphatidylinositol 4,5-bisphosphate, cholesterol, and fatty acids modulate the calcium-activated chloride channel TMEM16A (ANO1), Biochim Biophys Acta Mol Cell Biol Lipids, 1863, 299, 10.1016/j.bbalip.2017.12.009
Currie, 1995, Activation of Ca(2+)-dependent Cl-currents in cultured rat sensory neurones by flash photolysis of DM-nitrophen, J Physiol, 482, 291, 10.1113/jphysiol.1995.sp020518
Large, 1996, Characteristics and physiological role of the Ca(2+)-activated Cl-conductance in smooth muscle, Am J Physiol, 271, 435, 10.1152/ajpcell.1996.271.2.C435
Nilius, 1997, Calcium-activated chloride channels in bovine pulmonary artery endothelial cells, J Physiol, 498, 381, 10.1113/jphysiol.1997.sp021865
Zygmunt, 1994, Intracellular calcium activates a chloride current in canine ventricular myocytes, Am J Physiol, 267, H1984
Loretta, 2009, Regulation of TMEM16A chloride channel properties by alternative splicing, J Biol Chem, 284, 33360, 10.1074/jbc.M109.046607
Hartzell, 2005, Calcium-activated chloride channels, Annu Rev Physiol, 67, 719, 10.1146/annurev.physiol.67.032003.154341
Huang, 2012, International union of basic and clinical pharmacology. LXXXV: calcium-activated chloride channels, Pharmacol Rev, 64, 1, 10.1124/pr.111.005009
Pedemonte, 2014, Structure and function of TMEM16 proteins (anoctamins), Physiol Rev, 94, 419, 10.1152/physrev.00039.2011
Verkman, 2006, CFTR chloride channel drug discovery – inhibitors as antidiarrheals and activators for therapy of cystic fibrosis, Curr Pharm Des, 12, 2235, 10.2174/138161206777585148
Sondo, 2014, The TMEM16A chloride channel as an alternative therapeutic target in cystic fibrosis, Int J Biochem Cell Biol, 52, 73, 10.1016/j.biocel.2014.03.022
Malysz, 2017, Conditional genetic deletion of Ano1 in interstitial cells of Cajal impairs Ca(2+) transients and slow waves in adult mouse small intestine, Am J Physiol Gastrointest Liver Physiol, 312, G228, 10.1152/ajpgi.00363.2016
Singh, 2014, Ano1, a Ca2+-activated Cl- channel, coordinates contractility in mouse intestine by Ca2+ transient coordination between interstitial cells of Cajal, J Physiol, 592, 4051, 10.1113/jphysiol.2014.277152
Lee, 2014, Anoctamin 1 contributes to inflammatory and nerve-injury induced hypersensitivity, Mol Pain, 10, 5
Dixit, 2015, TMEM16A/ANO1 is differentially expressed in HPV-negative versus HPV-positive head and neck squamous cell carcinoma through promoter methylation, Sci Rep, 5, 16657, 10.1038/srep16657
Liu, 2015, TMEM16A overexpression contributes to tumor invasion and poor prognosis of human gastric cancer through TGF-beta signaling, Oncotarget, 6, 11585, 10.18632/oncotarget.3412
Espinosa, 2008, A novel monoclonal antibody against DOG1 is a sensitive and specific marker for gastrointestinal stromal tumors, Am J Surg Pathol, 32, 210, 10.1097/PAS.0b013e3181238cec
Sui, 2014, Inhibition of TMEM16A expression suppresses growth and invasion in human colorectal cancer cells, PLoS ONE, 9, 10.1371/journal.pone.0115443
Jia, 2015, Inhibition of calcium-activated chloride channel ANO1/TMEM16A suppresses tumor growth and invasion in human lung cancer, PLoS ONE, 10, 10.1371/journal.pone.0136584
Liu, 2019, Inhibition of Ca2+-activated chloride channel ANO1 suppresses ovarian cancer through inactivating PI3K/Akt signaling, Int J Cancer, 144, 2215, 10.1002/ijc.31887
Lee, 2018, Prediction of novel anoctamin1 (ANO1) inhibitors using 3D-QSAR pharmacophore modeling and molecular docking, Int J Mol Sci, 19(10)
Paulino, 2017, Structural basis for anion conduction in the calcium-activated chloride channel TMEM16A, Elife, 6
Dang, 2017, Cryo-EM structures of the TMEM16A calcium-activated chloride channel, Nature, 552, 426, 10.1038/nature25024
Paulino, 2017, Activation mechanism of the calcium-activated chloride channel TMEM16A revealed by cryo-EM, Nature, 552, 421, 10.1038/nature24652
Sondo, 2014, Non-canonical translation start sites in the TMEM16A chloride channel, Biochim Biophys Acta (BBA) – Biomembranes, 1838, 89, 10.1016/j.bbamem.2013.08.010
Ferrera, 2009, Regulation of TMEM16A chloride channel properties by alternative splicing, J Biol Chem, 284, 33360, 10.1074/jbc.M109.046607
Boese, 2004, Kinetics and regulation of a Ca2+-activated Cl- conductance in mouse renal inner medullary collecting duct cells, Am J Physiol Renal Physiol, 286, F682, 10.1152/ajprenal.00123.2003
Qu, 2003, Characterization of Ca2+-activated Cl- currents in mouse kidney inner medullary collecting duct cells, Am J Physiol Renal Physiol, 285, F326, 10.1152/ajprenal.00034.2003
Tien, 2014, A comprehensive search for calcium binding sites critical for TMEM16A calcium-activated chloride channel activity, Elife, 3
Pang, 2015, Molecular simulation assisted identification of Ca(2+) binding residues in TMEM16A, J Comput Aided Mol Des, 29, 1035, 10.1007/s10822-015-9876-x
Yu, 2012, Explaining calcium-dependent gating of anoctamin-1 chloride channels requires a revised topology, Circ Res, 110, 990, 10.1161/CIRCRESAHA.112.264440
Bushell, 2019, The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K, Nat Commun, 10, 3956, 10.1038/s41467-019-11753-1
Guan, 2017, Allosteric-activation mechanism of BK channel gating ring triggered by calcium ions, PLoS ONE, 12(9)
Pang, 2013, Combining fragment homology modeling with molecular dynamics aims at prediction of Ca(2)(+) binding sites in CaBPs, J Comput Aided Mol Des, 27, 697, 10.1007/s10822-013-9668-0
Falzone, 2019, Structural basis of Ca2+-dependent activation and lipid transport by a TMEM16 scramblase, Elife, 8, 10.7554/eLife.43229
Feng, S., et al., Cryo-EM studies of TMEM16F calcium-activated ion channel suggest features important for lipid scrambling. Cell Rep, 2019. 28(2): p. 567–579 e4.
Kalienkova, 2019, Stepwise activation mechanism of the scramblase nhTMEM16 revealed by cryo-EM, Elife, 8, 10.7554/eLife.44364
Peters, 2015, Four basic residues critical for the ion selectivity and pore blocker sensitivity of TMEM16A calcium-activated chloride channels, Proc Natl Acad Sci U S A, 112, 3547, 10.1073/pnas.1502291112
Mclaughlin, 2002, PIP(2) and proteins: interactions, organization, and information flow, Annu Rev Biophys Biomol Struct, 31, 151, 10.1146/annurev.biophys.31.082901.134259
Logothetis, 2015, Phosphoinositide control of membrane protein function: a frontier led by studies on ion channels, Annu Rev Physiol, 77, 81, 10.1146/annurev-physiol-021113-170358
De Jesús-Pérez, 2017, Phosphatidylinositol 4,5-bisphosphate, cholesterol, and fatty acids modulate the calcium-activated chloride channel TMEM16A (ANO1), Biochim Biophys Acta (BBA) – Mol Cell Biol Lipids
Ta, 2017, Contrasting effects of phosphatidylinositol 4,5-bisphosphate on cloned TMEM16A and TMEM16B channels, Br J Pharmacol, 174, 2984, 10.1111/bph.13913
Suh, 2008, PIP2 is a necessary cofactor for ion channel function: how and why?, Annu Rev Biophys, 37, 175, 10.1146/annurev.biophys.37.032807.125859
Peters, C.J., et al., The sixth transmembrane segment is a major gating component of the TMEM16A calcium-activated chloride channel. Neuron, 2018. 97(5): p. 1063–1077 e4.
Lam, 2018, Calcium-dependent electrostatic control of anion access to the pore of the calcium-activated chloride channel TMEM16A, Elife, 7
Alvadia, 2019, Cryo-EM structures and functional characterization of the murine lipid scramblase TMEM16F, Elife, 8, 10.7554/eLife.44365
Ji, 2019, Recent advances in TMEM16A: structure, function, and disease, J Cell Physiol, 234, 7856, 10.1002/jcp.27865
Guo, 2019, Entering the spotlight: chitosan oligosaccharides as novel activators of CaCCs/TMEM16A, Pharmacol Res, 146, 10.1016/j.phrs.2019.104323
Chai, 2017, Identification of resveratrol, an herbal compound, as an activator of the calcium-activated chloride channel, TMEM16A, J Membr Biol, 250, 483, 10.1007/s00232-017-9975-9
Guo, 2017, Ginsenoside Rb1, a novel activator of the TMEM16A chloride channel, augments the contraction of guinea pig ileum, Pflugers Arch, 469, 681, 10.1007/s00424-017-1934-x
Huang, 2012, Calcium-activated chloride channel TMEM16A modulates mucin secretion and airway smooth muscle contraction, Proc Natl Acad Sci U S A, 109, 16354, 10.1073/pnas.1214596109
Guadalupe, 2018, Blockade of anoctamin-1 in injured and uninjured nerves reduces neuropathic pain, Brain Res, 1696, 38, 10.1016/j.brainres.2018.06.001
Guo, 2019, Matrine is a novel inhibitor of the TMEM16A chloride channel with antilung adenocarcinoma effects, J Cell Physiol, 234, 8698, 10.1002/jcp.27529
Guo, 2020, The molecular mechanism of ginsenoside analogs activating TMEM16A, Biophys J, 118, 262, 10.1016/j.bpj.2019.11.015
Nagai, 2002, A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications, Nat Biotechnol, 20, 87, 10.1038/nbt0102-87
Sliwoski, 2014, Computational methods in drug discovery, Pharmacol Rev, 66, 334, 10.1124/pr.112.007336