Structural order in Pannexin 1 cytoplasmic domains

References

• Panchin Y, Kelmanson I, Matz M, Lukyanov K, Usman N, Lukyanov S. A ubiquitous family of putative gap junction molecules. Curr Biol 2000; 10:R473 - 4; http://dx.doi.org/10.1016/S0960-9822(00)00576-5; PMID: 10898987
   PubMed Web of Science ®Google Scholar
• Boassa D, Ambrosi C, Qiu F, Dahl G, Gaietta G, Sosinsky G. Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane. J Biol Chem 2007; 282:31733 - 43; http://dx.doi.org/10.1074/jbc.M702422200; PMID: 17715132
   PubMed Web of Science ®Google Scholar
• Ambrosi C, Gassmann O, Pranskevich JN, Boassa D, Smock A, Wang J, Dahl G, Steinem C, Sosinsky GE. Pannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other. J Biol Chem 2010; 285:24420 - 31; http://dx.doi.org/10.1074/jbc.M110.115444; PMID: 20516070
   PubMed Web of Science ®Google Scholar
• Vanden Abeele F, Bidaux G, Gordienko D, Beck B, Panchin YV, Baranova AV, Ivanov DV, Skryma R, Prevarskaya N. Functional implications of calcium permeability of the channel formed by pannexin 1. J Cell Biol 2006; 174:535 - 46; http://dx.doi.org/10.1083/jcb.200601115; PMID: 16908669
   PubMed Web of Science ®Google Scholar
• Iglesias R, Dahl G, Qiu F, Spray DC, Scemes E. Pannexin 1: the molecular substrate of astrocyte “hemichannels”. J Neurosci 2009; 29:7092 - 7; http://dx.doi.org/10.1523/JNEUROSCI.6062-08.2009; PMID: 19474335
   PubMed Web of Science ®Google Scholar
• Bao L, Locovei S, Dahl G. Pannexin membrane channels are mechanosensitive conduits for ATP. FEBS Lett 2004; 572:65 - 8; http://dx.doi.org/10.1016/j.febslet.2004.07.009; PMID: 15304325
   PubMed Web of Science ®Google Scholar
• Unger VM, Kumar NM, Gilula NB, Yeager M. Three-dimensional structure of a recombinant gap junction membrane channel. Science 1999; 283:1176 - 80; http://dx.doi.org/10.1126/science.283.5405.1176; PMID: 10024245
   PubMed Web of Science ®Google Scholar
• Epstein ML, Gilula NB. A study of communication specificity between cells in culture. J Cell Biol 1977; 75:769 - 87; http://dx.doi.org/10.1083/jcb.75.3.769; PMID: 562887
   PubMed Web of Science ®Google Scholar
• Moreno AP, Chanson M, Elenes S, Anumonwo J, Scerri I, Gu H, Taffet SM, Delmar M. Role of the carboxyl terminal of connexin43 in transjunctional fast voltage gating. Circ Res 2002; 90:450 - 7; http://dx.doi.org/10.1161/hh0402.105667; PMID: 11884375
   PubMed Web of Science ®Google Scholar
• Hirst-Jensen BJ, Sahoo P, Kieken F, Delmar M, Sorgen PL. Characterization of the pH-dependent interaction between the gap junction protein connexin43 carboxyl terminus and cytoplasmic loop domains. J Biol Chem 2007; 282:5801 - 13; http://dx.doi.org/10.1074/jbc.M605233200; PMID: 17178730
   PubMed Web of Science ®Google Scholar
• Duffy HS, Sorgen PL, Girvin ME, O’Donnell P, Coombs W, Taffet SM, Delmar M, Spray DC. pH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains. J Biol Chem 2002; 277:36706 - 14; http://dx.doi.org/10.1074/jbc.M207016200; PMID: 12151412
   PubMed Web of Science ®Google Scholar
• Solan JL, Marquez-Rosado L, Sorgen PL, Thornton PJ, Gafken PR, Lampe PD. Phosphorylation at S365 is a gatekeeper event that changes the structure of Cx43 and prevents down-regulation by PKC. J Cell Biol 2007; 179:1301 - 9; http://dx.doi.org/10.1083/jcb.200707060; PMID: 18086922
   PubMed Web of Science ®Google Scholar
• Chekeni FB, Elliott MR, Sandilos JK, Walk SF, Kinchen JM, Lazarowski ER, Armstrong AJ, Penuela S, Laird DW, Salvesen GS, et al. Pannexin 1 channels mediate ‘find-me’ signal release and membrane permeability during apoptosis. Nature 2010; 467:863 - 7; http://dx.doi.org/10.1038/nature09413; PMID: 20944749
   PubMed Web of Science ®Google Scholar
• Sandilos JK, Chiu YH, Chekeni FB, Armstrong AJ, Walk SF, Ravichandran KS, Bayliss DA. Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region. J Biol Chem 2012; 287:11303 - 11; http://dx.doi.org/10.1074/jbc.M111.323378; PMID: 22311983
   PubMed Web of Science ®Google Scholar
• Penuela S, Bhalla R, Gong XQ, Cowan KN, Celetti SJ, Cowan BJ, Bai D, Shao Q, Laird DW. Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins. J Cell Sci 2007; 120:3772 - 83; http://dx.doi.org/10.1242/jcs.009514; PMID: 17925379
   PubMedGoogle Scholar
• Barbe MT, Monyer H, Bruzzone R. Cell-cell communication beyond connexins: the pannexin channels. Physiology (Bethesda) 2006; 21:103 - 14; http://dx.doi.org/10.1152/physiol.00048.2005; PMID: 16565476
   PubMed Web of Science ®Google Scholar
• Weilinger NL, Tang PL, Thompson RJ. Anoxia-induced NMDA receptor activation opens pannexin channels via Src family kinases. J Neurosci 2012; 32:12579 - 88; http://dx.doi.org/10.1523/JNEUROSCI.1267-12.2012; PMID: 22956847
   PubMed Web of Science ®Google Scholar
• Iglesias R, Locovei S, Roque A, Alberto AP, Dahl G, Spray DC, Scemes E. P2X7 receptor-Pannexin1 complex: pharmacology and signaling. Am J Physiol Cell Physiol 2008; 295:C752 - 60; http://dx.doi.org/10.1152/ajpcell.00228.2008; PMID: 18596211
   PubMed Web of Science ®Google Scholar
• Riquelme MA, Cea LA, Vega JL, Boric MP, Monyer H, Bennett MV, Frank M, Willecke K, Sáez JC. The ATP required for potentiation of skeletal muscle contraction is released via pannexin hemichannels. Neuropharmacology 2013; 75:594 - 603; http://dx.doi.org/10.1016/j.neuropharm.2013.03.022; PMID: 23583931
   PubMed Web of Science ®Google Scholar
• Hessa T, Meindl-Beinker NM, Bernsel A, Kim H, Sato Y, Lerch-Bader M, Nilsson I, White SH, von Heijne G. Molecular code for transmembrane-helix recognition by the Sec61 translocon. Nature 2007; 450:1026 - 30; http://dx.doi.org/10.1038/nature06387; PMID: 18075582
   PubMed Web of Science ®Google Scholar
• Hofmann K, Stoffel W. TMBASE - A database of membrane spanning protein segments. Biol Chem Hoppe Seyler 1993; 374:166
   Google Scholar
• Cserzö M, Wallin E, Simon I, von Heijne G, Elofsson A. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng 1997; 10:673 - 6; http://dx.doi.org/10.1093/protein/10.6.673; PMID: 9278280
   PubMedGoogle Scholar
• von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J Mol Biol 1992; 225:487 - 94; http://dx.doi.org/10.1016/0022-2836(92)90934-C; PMID: 1593632
   PubMed Web of Science ®Google Scholar
• Wang J, Dahl G. SCAM analysis of Panx1 suggests a peculiar pore structure. J Gen Physiol 2010; 136:515 - 27; http://dx.doi.org/10.1085/jgp.201010440; PMID: 20937692
   PubMed Web of Science ®Google Scholar
• Garnier J, Gibrat JF, Robson B. GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol 1996; 266:540 - 53; http://dx.doi.org/10.1016/S0076-6879(96)66034-0; PMID: 8743705
   PubMed Web of Science ®Google Scholar
• Cole C, Barber JD, Barton GJ. The Jpred 3 secondary structure prediction server. Nucleic Acids Res 2008; 36:W197-201; http://dx.doi.org/10.1093/nar/gkn238; PMID: 18463136
   PubMedGoogle Scholar
• Rost B, Yachdav G, Liu J. The PredictProtein server. Nucleic Acids Res 2004; 32:W321-6; http://dx.doi.org/10.1093/nar/gkh377; PMID: 15215403
   PubMedGoogle Scholar
• Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999; 292:195 - 202; http://dx.doi.org/10.1006/jmbi.1999.3091; PMID: 10493868
   PubMed Web of Science ®Google Scholar
• Fort AG, Spray DC. Trifluoroethanol reveals helical propensity at analogous positions in cytoplasmic domains of three connexins. Biopolymers 2009; 92:173 - 82; http://dx.doi.org/10.1002/bip.21166; PMID: 19226516
   PubMed Web of Science ®Google Scholar
• Sönnichsen FD, Van Eyk JE, Hodges RS, Sykes BD. Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 1992; 31:8790 - 8; http://dx.doi.org/10.1021/bi00152a015; PMID: 1390666
   PubMed Web of Science ®Google Scholar
• Kentsis A, Sosnick TR. Trifluoroethanol promotes helix formation by destabilizing backbone exposure: desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding. Biochemistry 1998; 37:14613 - 22; http://dx.doi.org/10.1021/bi981641y; PMID: 9772190
   PubMed Web of Science ®Google Scholar
• Ramírez-Alvarado M, Kortemme T, Blanco FJ, Serrano L. Beta-hairpin and beta-sheet formation in designed linear peptides. Bioorg Med Chem 1999; 7:93 - 103; http://dx.doi.org/10.1016/S0968-0896(98)00215-6; PMID: 10199660
   PubMed Web of Science ®Google Scholar
• Blanco FJ, Serrano L. Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements. Eur J Biochem 1995; 230:634 - 49; http://dx.doi.org/10.1111/j.1432-1033.1995.tb20605.x; PMID: 7607238
   PubMedGoogle Scholar
• Reiersen H, Rees AR. Trifluoroethanol may form a solvent matrix for assisted hydrophobic interactions between peptide side chains. Protein Eng 2000; 13:739 - 43; http://dx.doi.org/10.1093/protein/13.11.739; PMID: 11161104
   PubMedGoogle Scholar
• Brahms S, Brahms J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J Mol Biol 1980; 138:149 - 78; http://dx.doi.org/10.1016/0022-2836(80)90282-X; PMID: 7411608
   PubMed Web of Science ®Google Scholar
• Wishart DS, Sykes BD. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 1994; 4:171 - 80; http://dx.doi.org/10.1007/BF00175245; PMID: 8019132
   PubMed Web of Science ®Google Scholar
• Johns SJ. TOPO2, transmembrane protein display software, http://www.sacs.ucsf.edu/TOPO2/
   Google Scholar
• Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC. Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. J Biol Chem 2004; 279:54695 - 701; http://dx.doi.org/10.1074/jbc.M409552200; PMID: 15492000
   PubMed Web of Science ®Google Scholar
• Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. J Biol Chem 2009; 284:34257 - 71; http://dx.doi.org/10.1074/jbc.M109.039594; PMID: 19808665
   PubMed Web of Science ®Google Scholar
• Kopanic JL, Sorgen PL. Chemical shift assignments of the connexin45 carboxyl terminal domain: monomer and dimer conformations. Biomol NMR Assign 2013; 7:293 - 7; http://dx.doi.org/10.1007/s12104-012-9431-9; PMID: 23070843
   PubMed Web of Science ®Google Scholar
• Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R. The open pore conformation of potassium channels. Nature 2002; 417:523 - 6; http://dx.doi.org/10.1038/417523a; PMID: 12037560
   PubMed Web of Science ®Google Scholar
• Traynelis SF, Wollmuth LP, McBain CJ, Menniti FS, Vance KM, Ogden KK, Hansen KB, Yuan H, Myers SJ, Dingledine R. Glutamate receptor ion channels: structure, regulation, and function. Pharmacol Rev 2010; 62:405 - 96; http://dx.doi.org/10.1124/pr.109.002451; PMID: 20716669
   PubMed Web of Science ®Google Scholar
• Bao L, Locovei S, Dahl G. Pannexin membrane channels are mechanosensitive conduits for ATP. FEBS Lett 2004; 572:65 - 8; http://dx.doi.org/10.1016/j.febslet.2004.07.009; PMID: 15304325
   PubMed Web of Science ®Google Scholar
• Locovei S, Wang J, Dahl G. Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium. FEBS Lett 2006; 580:239 - 44; http://dx.doi.org/10.1016/j.febslet.2005.12.004; PMID: 16364313
   PubMed Web of Science ®Google Scholar
• Sandilos JK, Bayliss DA. Physiological mechanisms for the modulation of pannexin 1 channel activity. J Physiol 2012; 590:6257 - 66; http://dx.doi.org/10.1113/jphysiol.2012.240911; PMID: 23070703
   PubMed Web of Science ®Google Scholar
• Kieken F, Spagnol G, Su V, Lau AF, Sorgen PL. NMR structure note: UBA domain of CIP75. J Biomol NMR 2010; 46:245 - 50; http://dx.doi.org/10.1007/s10858-010-9397-9; PMID: 20127391
   PubMed Web of Science ®Google Scholar
• Sorgen PL, Duffy HS, Cahill SM, Coombs W, Spray DC, Delmar M, Girvin ME. Sequence-specific resonance assignment of the carboxyl terminal domain of Connexin43. J Biomol NMR 2002; 23:245 - 6; http://dx.doi.org/10.1023/A:1019892719979; PMID: 12238598
   PubMed Web of Science ®Google Scholar
• Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 1995; 6:277 - 93; http://dx.doi.org/10.1007/BF00197809; PMID: 8520220
   PubMed Web of Science ®Google Scholar
• Johnson BA, Blevins RA. NMR View: A computer program for the visualization and analysis of NMR data. J Biomol NMR 1994; 4:603 - 14; http://dx.doi.org/10.1007/BF00404272; PMID: 22911360
   PubMed Web of Science ®Google Scholar