Abstract
Ion channels are involved in the depolarization and repolarization of excitable membranes, excitation contraction coupling, etc. They can be divided into groups based upon biophysical, electrophysiological, and pharmacological properties (Hille 1984). Recent cloning and sequencing of some ion channel polypeptides has permitted initial attempts to correlate ion channel structure and function. These efforts have revealed that sodium channel α1 and dihydropyridine-sensitive calcium channel α1 polypeptides have recognizably similar amino acid sequences, both of which appear to have evolved by two gene duplications from an ancient ion channel probably resembling the Drosophila Shaker gene product, a voltage-gated potassium channel (Trimmer and Agnew 1989; Ramaswami and Tanouye 1989).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Auld VJ, Goldin AL, Krqafte DS, Marshall J, Dunn JM, Catterall WA, Lester HA, Davidson N, Dunn RJ (1988) A rat brain Na+ channel a subunit with novel gating properties. Neuron 1:449–461.
Babitch JA (1988) On calcium binding to channel proteins. J theor Biol. 133:525–528.
Babitch JA, Anthony FA (1987) Grasping for calcium binding sites in sodium channels with an EF hand. J theor Biol 127:451–459.
Bajorath J, Raghunathan S, Hinrichs W, Saenger W (1989) Long-range structural changes in proteinase K triggered by calcium ion removal. Nature 337:481–484.
Baumann A, Krah-Jentgens I, Müller R, Müller-Holtkamp F, Seidel R, Kecskemethy N, Casal J, Ferrus A, Pongs O (1987) Molecular organization of the maternal effect region of the Shaker complex of Drosophila: characterization of an IA channel transcript with homology to vertebrate Na+ channel. EMBO J 6:3419–3429.
Baumann A, Grape A, Ackermann A, Pongs O (1988) Structure of the voltage-dependent potassium channel is highly conserved from Drosophila to vertebrate central nervous systems. EMBO J 7:2457–2463.
Buisson G, Duee E, Haser R, Payan F (1987) Three dimensional structure of porcine pancreatic α-amylase at 2.9Å resolution. Role of calcium in structure and activity. EMBO J 6:3909–3916.
Butler A, Wei A, Baker K, Salkoff L (1989) A family of putative potassium channel genes in Drosophila. Science 243:943–947.
Calabretta B, Battini R, Kaczmarek L, de Riel JK, Baserga R (1986) Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein. J Biol Chem 261:12628–12632.
Ellis SB, Williams ME, Ways NR, Brenner R, Sharp AH, Leung AT, Campbell KP, McKenna E, Koch WJ, Hui A, Schwartz A, Harpold MM (1988) Sequence and expression of mRNAs encoding the α1 and α2 subunits of a DHP-sensitive calcium channel. Science 241:1661–1664.
Hille B (1984) Ionic Channels of Excitable Membranes. Sinauer, Sutherland, MA.
Kayano T, Noda M, Flockerzi V, Takahashi H, Numa S (1988) Primary structure of rat brain sodium channel in deduced from the cDNA sequence. FEBS Lett 228:187–194.
Koch WJ, Hui A, Shul GE, Ellinor P, Schwartz A (1989) Characterization of cDNA clones encoding two putative isoforms of the α1 subunit of the dihydropyridine-sensitive voltage-dependent calcium channel isolated from rat brain and rat aorta. FEBS Lett 250:386–388.
Linse S, Brodin P, Johansson C, Thulin E, Grandström T, Forsén S (1988) The role of protein surface charges in ion binding. Nature 335:651–652.
Loughney K, Kreber R, Ganetzky B (1989) Molecular analysis of the para locus, a sodium channel gene in Drosophila. Cell 58:1143–1154.
McKinnon D (1989) Isolation of a cDNA clone coding for a putative second potassium channel indicates the existence of a gene family. J Biol Chem 264:8230–8236.
Mikami A, Imoto K, Tanabe T, Niidome T, Mori Y, Takeshima H, Narumiya S, Numa S (1989) Primary structure and functional expression of the cardiac dihydropyridine-sensitive calcium channel. Nature 340:230–233.
Murai T, Kakizuka A, Takumi T, Ohkubo H, Nakanishi S (1989) Molecular cloning and sequence analysis of human genomic DNA encoding a novel membrane protein which exhibits a slowly activating potassium channel activity. Biochem Biophys Res Commun 161:176–181.
Noda M, Shimizu S, Tanabe T, Takai T, Kayano T, Ikeda T, Takahashi H, Nakayama H, Kanaoka Y, Minamino N, Kangawa K, Matsuo H, Raftery MA, Hirose T, Inayama S, Hayashida H, Miyata T, Numa S (1984). Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence. Nature 312:121–127.
Noda M, Ikeda T, Kayano T, Suzuki H, Takeshima H, Kurasaki M, Takahashi H, Numa S (1986) Existence of distinct sodium channel messenger RNAs in rat brain. Nature 320:188–192.
Pongs O, Kecskemethy N, Müller R, Krah-Jentgens I, Baumann A, Kiltz HH, Canal I, Llamazares S, Ferras A (1988) Shaker encodes a family of putative potassium channel proteins in the nervous system of Drosophila. EMBO J 7:1087–1096.
Ramaswami M, Tanouye MA (1989) Two sodium-channel genes in Drosophila: implications for channel diversity. Proc Natl Acad Sci USA 86:2079–2082.
Rogart RB, Cribbs LL, Muglia LK, Kephart DD, Kaiser MW (1989) Molecular cloning of a putative tetrodotoxin-resistant rat heart Na+ channel isoform. Proc Natl Acad Sci USA 86:8170–8174.
Ruth P, Rohrkasten A, Biel M, Bosse E, Regulla S, Meyer HE, Flockerzi V, Hofmann F (1989) Primary structure of the beta subunit of the DHP-sensitive calcium channel from skeletal muscle. Science 245:1115–1118.
Salkoff L, Butler A, Scavarda N, Wei A (1987a) Nucleotide sequence of the putative sodium channel gene from Drosophila: the four homologous domains. Nucleic Acids Res 15:8569–8572.
Salkoff L, Butler A, Wei A, Scavarda N, Giffen K, Ifune C, Goodman R, Mandel G (1987b) Genomic organization and deduced amino acid sequence of a putative sodium channel gene in Drosophila. Science 237:744–749.
Schwarz TL, Tempel BL, Papazian DM, Jan YN, Jan LY (1988) Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila. Nature 331:137–142.
Scott BT, Simmerman HKB, Collins JH, Nadal-Ginard B, Jones LR (1988) Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning. J Biol Chem 263:8958–8964.
Slish DF, Engle DB, Varadi G, Lotan I, Singer D, Dascal N, Schwartz A (1989) Evidence for the existence of a cardiac specific isoform of the α1 subunit of the voltage dependent calcium channel. FEBS Lett 250:509–514.
Stuart DI, Acharya KR, Walker NPC, Smith SG, Lewis, M, Phillips DC (1986) α-Lactalbumin possesses a novel calcium binding loop. Nature 324:84–87.
Takumi T, Ohkubo H, Nakanishi S (1988) Cloning of a membrane protein that induces a slow voltage-gated potassium current. Science 242:1042–1045.
Tanabe T, Takeshima H, Mikami A, Flockerzi V, Takahashi H, Kangawa K, Kojima M, Matsuo H, Hirose T, Numa S (1987) Primary structure of the receptor for calcium channel blockers from skeletal muscle. Nature 328:313–318.
Temple BL, Jan YN, Jan LY (1988) Cloning of a probable potassium channel gene from mouse brain. Nature 332:837–839.
Trimmer JS, Agnew WS (1989) Molecular diversity of voltage-sensitive Na channels. Annu Rev Physiol 51:401–418.
Trimmer JS, Cooperman SS, Tomiko SA, Zhou J, Crean SM, Boyle MB, Kallen RG, Sheng Z, Barchi RL, Sigworth FJ, Goodman RH, Agnew WS, Mandel G (1989) Primary structure and functional expression of a mammalian skeletal muscle sodium channel. Neuron 3:33–49.
Tufty RM, Kretsinger RH (1975) Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. Science 187:167–169.
Vyas MN, Jacobson BL, Quiocho FA (1989) The calcium-binding site in the galactose chemoreceptor protein. Crystallographic and metal binding studies. J Biol Chem 264:20817–20821.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1991 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Babitch, J.A. (1991). Putative Calcium-Binding Sites in Voltage-Gated Sodium and Calcium Channel α1 Subunits. In: Heizmann, C.W. (eds) Novel Calcium-Binding Proteins. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76150-8_31
Download citation
DOI: https://doi.org/10.1007/978-3-642-76150-8_31
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-76152-2
Online ISBN: 978-3-642-76150-8
eBook Packages: Springer Book Archive