Ion Channels

  • Angelika BöttgerEmail author
  • Ute Vothknecht
  • Cordelia Bolle
  • Alexander Wolf
Part of the Learning Materials in Biosciences book series (LMB)


Ion channels are formed by proteins with multiple, usually six, transmembrane domains, which as homo- or hetero-oligomers form aqueous pores that allow ions to pass between the outside and the inside of the cell according to their concentration gradient. Ion channels thus conduct ion currents in response to changes in membrane voltage (voltage-gated ion channels) or after binding of ligands (ligand gated). The latter applies to neurotransmitters binding at extracellular sites and to second messengers binding at intracellular sites of the channel oligomers. In the following, we discuss how the membrane potential is maintained and explain the molecular architecture and function of several ion channels. As an example, we elucidate, how voltage- and ligand-gated ion channels work together at the neuromuscular junction and at synapses. Finally, we briefly introduce the large family of “transient receptor potential” (TRP) ion channels.


  1. Berridge MJ (2012) Calcium signalling remodelling and disease. Biochem Soc Trans 40:297–309CrossRefGoogle Scholar
  2. Bichet D, Haass FA, Jan LY (2003) Merging functional studies with structures of inward-rectifier K(+) channels. Nat Rev Neurosci 4:957–967CrossRefGoogle Scholar
  3. Catterall WA (2000) From ionic currents to molecular mechanisms: the structure and function of voltage-gated sodium channels. Neuron 26:13–25CrossRefGoogle Scholar
  4. Cestele S, Catterall WA (2000) Molecular mechanisms of neurotoxin action on voltage-gated sodium channels. Biochimie 82:883–892CrossRefGoogle Scholar
  5. Civelli O (2012) Orphan GPCRs and neuromodulation. Neuron 76:12–21CrossRefGoogle Scholar
  6. Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stuhmer W, Wang X (2005) International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels. Pharmacol Rev 57:473–508CrossRefGoogle Scholar
  7. Huang W, Liu M, Yan SF, Yan N (2017) Structure-based assessment of disease-related mutations in human voltage-gated sodium channels. Protein Cell 8:401–438CrossRefGoogle Scholar
  8. Isomoto S, Kondo C, Kurachi Y (1997) Inwardly rectifying potassium channels: their molecular heterogeneity and function. Jpn J Physiol 47:11–39CrossRefGoogle Scholar
  9. Labro AJ, Snyders DJ (2012) Being flexible: the voltage-controllable activation gate of kv channels. Front Pharmacol 3:168CrossRefGoogle Scholar
  10. Li Q, Wanderling S, Paduch M, Medovoy D, Singharoy A, McGreevy R, Villalba-Galea CA, Hulse RE, Roux B, Schulten K, Kossiakoff A, Perozo E (2014) Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain. Nat Struct Mol Biol 21:244–252CrossRefGoogle Scholar
  11. Luscher C, Slesinger PA (2010) Emerging roles for G protein-gated inwardly rectifying potassium (GIRK) channels in health and disease. Nat Rev Neurosci 11:301–315CrossRefGoogle Scholar
  12. Nozaki T, Ozawa SI, Harada H, Kimura T, Osawa M, Shimada I (2016) Disulfide mapping the voltage-sensing mechanism of a voltage-dependent potassium channel. Sci Rep 6:37303CrossRefGoogle Scholar
  13. Nys M, Kesters D, Ulens C (2013) Structural insights into Cys-loop receptor function and ligand recognition. Biochem Pharmacol 86:1042–1053CrossRefGoogle Scholar
  14. Shen H, Zhou Q, Pan X, Li Z, Wu J, Yan N (2017) Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution. Science 355:1Google Scholar
  15. Skou JC, Esmann M (1992) The Na,K-ATPase. J Bioenerg Biomembr 24:249–261PubMedGoogle Scholar
  16. Sokolova O, Kolmakova-Partensky L, Grigorieff N (2001) Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution. Structure 9:215–220CrossRefGoogle Scholar
  17. Van Petegem F (2012) Ryanodine receptors: structure and function. J Biol Chem 287:31624–31632CrossRefGoogle Scholar
  18. Zalk R, Lehnart SE, Marks AR (2007) Modulation of the ryanodine receptor and intracellular calcium. Annu Rev Biochem 76:367–385CrossRefGoogle Scholar

Copyright information

© Springer Nature Switzerland AG 2018

Authors and Affiliations

  • Angelika Böttger
    • 1
    Email author
  • Ute Vothknecht
    • 2
  • Cordelia Bolle
    • 3
  • Alexander Wolf
    • 4
  1. 1.Department Biology IILMU MunichPlanegg-MartinsriedGermany
  2. 2.IZMB-Plant Cell BiologyUniversity of BonnBonnGermany
  3. 3.Department Biology ILMU MunichPlanegg-MartinsriedGermany
  4. 4.Inst. Molecular Toxicology/PharmacologyHelmholtz Zentrum MünichNeuherbergGermany

Personalised recommendations