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      T-type channels buddy up

      review-article
      Author(s): ,
      Publication date (Electronic):
      Journal: Pflugers Archiv
      Publisher: Springer Berlin Heidelberg
      Keywords: Cav3, T-type, KCa3.1, KCa1.1, BK, Kv4, A-type

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          Abstract

          The electrical output of neurons relies critically on voltage- and calcium-gated ion channels. The traditional view of ion channels is that they operate independently of each other in the plasma membrane in a manner that could be predicted according to biophysical characteristics of the isolated current. However, there is increasing evidence that channels interact with each other not just functionally but also physically. This is exemplified in the case of Cav3 T-type calcium channels, where new work indicates the ability to form signaling complexes with different types of calcium-gated and even voltage-gated potassium channels. The formation of a Cav3-K complex provides the calcium source required to activate KCa1.1 or KCa3.1 channels and, furthermore, to bestow a calcium-dependent regulation of Kv4 channels via associated KChIP proteins. Here, we review these interactions and discuss their significance in the context of neuronal firing properties.

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          Molecular physiology of low-voltage-activated t-type calcium channels.

          Edward Perez-Reyes (2003)
          T-type Ca2+ channels were originally called low-voltage-activated (LVA) channels because they can be activated by small depolarizations of the plasma membrane. In many neurons Ca2+ influx through LVA channels triggers low-threshold spikes, which in turn triggers a burst of action potentials mediated by Na+ channels. Burst firing is thought to play an important role in the synchronized activity of the thalamus observed in absence epilepsy, but may also underlie a wider range of thalamocortical dysrhythmias. In addition to a pacemaker role, Ca2+ entry via T-type channels can directly regulate intracellular Ca2+ concentrations, which is an important second messenger for a variety of cellular processes. Molecular cloning revealed the existence of three T-type channel genes. The deduced amino acid sequence shows a similar four-repeat structure to that found in high-voltage-activated (HVA) Ca2+ channels, and Na+ channels, indicating that they are evolutionarily related. Hence, the alpha1-subunits of T-type channels are now designated Cav3. Although mRNAs for all three Cav3 subtypes are expressed in brain, they vary in terms of their peripheral expression, with Cav3.2 showing the widest expression. The electrophysiological activities of recombinant Cav3 channels are very similar to native T-type currents and can be differentiated from HVA channels by their activation at lower voltages, faster inactivation, slower deactivation, and smaller conductance of Ba2+. The Cav3 subtypes can be differentiated by their kinetics and sensitivity to block by Ni2+. The goal of this review is to provide a comprehensive description of T-type currents, their distribution, regulation, pharmacology, and cloning.
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            Small-conductance Ca2+-activated K+ channels: form and function.

            John Adelman, James Maylie, Pankaj Sah (2012)
            Small-conductance Ca(2+)-activated K(+) channels (SK channels) are widely expressed throughout the central nervous system. These channels are activated solely by increases in intracellular Ca(2+). SK channels are stable macromolecular complexes of the ion pore-forming subunits with calmodulin, which serves as the intrinsic Ca(2+) gating subunit, as well as with protein kinase CK2 and protein phosphatase 2A, which modulate Ca(2+) sensitivity. Well-known for their roles in regulating somatic excitability in central neurons, SK channels are also expressed in the postsynaptic membrane of glutamatergic synapses, where their activation and regulated trafficking modulate synaptic transmission and the induction and expression of synaptic plasticity, thereby affecting learning and memory. In this review we discuss the molecular and functional properties of SK channels and their physiological roles in central neurons.
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              Modulation of A-type potassium channels by a family of calcium sensors.

              Mark Bowlby, M Betty, James Trimmer … (2000)
              In the brain and heart, rapidly inactivating (A-type) voltage-gated potassium (Kv) currents operate at subthreshold membrane potentials to control the excitability of neurons and cardiac myocytes. Although pore-forming alpha-subunits of the Kv4, or Shal-related, channel family form A-type currents in heterologous cells, these differ significantly from native A-type currents. Here we describe three Kv channel-interacting proteins (KChIPs) that bind to the cytoplasmic amino termini of Kv4 alpha-subunits. We find that expression of KChIP and Kv4 together reconstitutes several features of native A-type currents by modulating the density, inactivation kinetics and rate of recovery from inactivation of Kv4 channels in heterologous cells. All three KChIPs co-localize and co-immunoprecipitate with brain Kv4 alpha-subunits, and are thus integral components of native Kv4 channel complexes. The KChIPs have four EF-hand-like domains and bind calcium ions. As the activity and density of neuronal A-type currents tightly control responses to excitatory synaptic inputs, these KChIPs may regulate A-type currents, and hence neuronal excitability, in response to changes in intracellular calcium.
              Article 0 comments Cited 144 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Ray W. Turner: +1-403-2208452 , +1-403-2107446 , rwturner@ucalgary.ca , http://www.acs.ucalgary.ca/∼rwturner
                Journal
                Journal ID (nlm-ta): Pflugers Arch
                Journal ID (iso-abbrev): Pflugers Arch
                Title: Pflugers Archiv
                Publisher: Springer Berlin Heidelberg (Berlin/Heidelberg )
                ISSN (Print): 0031-6768
                ISSN (Electronic): 1432-2013
                Publication date (Electronic): 11 January 2014
                Publication date PMC-release: 11 January 2014
                Publication date (Print): 2014
                Volume: 466
                Pages: 661-675
                Affiliations
                [ ]Department of Cell Biology and Anatomy, Hotchkiss Brain Institute, University of Calgary, HRIC Bldg, Room 1AA14, 3330 Hospital Dr. N.W., Calgary, T2N 4N1 Alberta Canada
                [ ]Department of Physiology and Pharmacology, Hotchkiss Brain Institute, University of Calgary, Calgary, T2N 4N1 Alberta Canada
                Article
                Publisher ID: 1434
                DOI: 10.1007/s00424-013-1434-6
                PMC ID: 3951889
                PubMed ID: 24413887
                SO-VID: 3c134802-eb94-4af5-9c4a-817d8529c0a6
                Copyright © © The Author(s) 2014
                License:

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.

                History
                Date received : 17 December 2013
                Date accepted : 23 December 2013
                Categories
                Subject: Invited Review
                Custom metadata
                issue-copyright-statement © Springer-Verlag Berlin Heidelberg 2014

                ScienceOpen disciplines: Anatomy & Physiology
                Keywords: cav3,t-type,kca3.1,kca1.1,bk,kv4,a-type
                Data availability:
                ScienceOpen disciplines: Anatomy & Physiology
                Keywords: cav3, t-type, kca3.1, kca1.1, bk, kv4, a-type

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