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Mikael Blomkvist
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This article is about the fictional character. For the American rower, see Michael Blomquist.
Mikael Blomkvist
Millennium character
Mikael Blomkvist, as portrayed by Michael Nyqvist in the Swedish film series.
First appearance
The Girl with the Dragon Tattoo
Last appearance
The Girl Who Takes an Eye for an Eye
Created by
Stieg Larsson
Portrayed by
Michael Nyqvist (Swedish)
Daniel Craig (English, 2011)
Sverrir Gudnason (English, 2018)
Information
Nickname(s)
Kalle Blomkvist
Gender
Male
Occupation
Journalist
Family
Kurt Blomkvist (father; deceased)
Anita Blomkvist (mother; deceased)
Annika Giannini (sister)
Enrico Giannini (brother-in-law)
Monica Abrahamson (ex-wife)
Pernilla Blomkvist (daughter)
Nationality
Swedish
Mikael Blomkvist is a fictional character created by Swedish author and journalist Stieg Larsson. He is a main character of Larsson's award-winning Millennium series, along with Lisbeth Salander.
Contents
1 Profile
1.1 Name
1.2 Overview
1.3 Character biography
1.4 Relationships
2 In film
3 References
Profile[edit]
Name[edit]
Larsson stated in interviews that he based many characters, including that of Lisbeth Salander, on characters from Astrid Lindgren novels.[1] Blomkvist is frequently referred to by his colleagues in the news media as "Kalle Blomkvist", a reference to a boy detective who appears in several of Lindgren's novels, because his first notable investigation is uncovering the hideout of a gang of bank robbers. Lisbeth Salander sarcastically refers to him by this nickname throughout the series.
Overview[edit]
"Mikael Blomkvist is a graduate of the School of Journalism and had much of his professional life dedicated to revealing and report suspicious transactions, specifically in the field of banking and business," writes Larsson in the first volume of the trilogy. "It will give the typical image of guardian of the moral, incorruptible, facing the business world. And as such quite frequently invite you to comment on various issues in television."
Character biography[edit]
Blomkvist is an investigative journalist and co-owner of the monthly magazine Millennium based in Stockholm, Sweden. At the start of The Girl with the Dragon Tattoo, he loses a libel case involving damaging allegations about billionaire industrialist Hans-Erik Wennerström, and is sentenced to three months in prison. Facing jail time and professional disgrace, Blomkvist steps down from his position on the magazine's board of directors. At the same time, he is offered a freelance assignment by Henrik Vanger, the former CEO of Vanger Enterprises and patriarch of the wealthy Vanger family, to help him solve the cold case of his great-niece, Harriet Vanger, who has been missing for 36 years and presumed dead. Blomkvist reluctantly accepts the case in exchange for valuable information Vanger claims to have that would help him in his case against Wennerström.
During this time, Blomkvist meets and begins to work with Salander, whom Vanger had hired prior to investigate Blomkvist while considering him for the job. The two form an important relationship, in which each of their skill-sets prove invaluable in solving the Vanger case; they also become lovers. At the end of the first novel, Salander saves Blomkvist from Vanger's great-nephew (and Harriet's brother) Martin, a serial killer who has been murdering women throughout Sweden for decades. Using her phone tapping contacts in London, she and Blomkvist discover that Harriet Vanger is alive and living in Australia. When Vanger's information about Wennerström proves to be useless, Salander uses her computer hacking skills to get sensitive information about Wennerström that is much more incriminating than what Blomkvist had in the past. With the information uncovered by Salander, Blomkvist publishes an exposé article and book that ruins Wennerström, clears his own name, and propels his magazine to one of the most respected and profitable in Sweden. Salander abruptly ends their relationship at the end of the novel, however, after seeing him with his lover and business partner, Erika Berger.
In the following novel, The Girl Who Played with Fire, two of Blomkvist's colleagues are murdered and Salander is identified as the prime suspect. Blomkvist becomes her only supporter and strives to clear her name, even as she wants nothing to do with him and refuses to help him in any way. He eventually discovers that the murders are part of an elaborate conspiracy between The Section—a faction of SÄPO, the Swedish Secret Service—and Salander's father, former Soviet spy Alexander Zalachenko, whom The Section had illegally helped to defect. He also learns that Salander was raped by one of the murder victims, Nils Bjurman, and that The Section conspired to have her committed to a mental hospital as a child in order to protect Zalachenko. He follows Salander to Zalachenko's farm, where he finds her near death after a confrontation with her father. He calls an ambulance, saving her life.
In the final novel of the original Millennium trilogy, The Girl Who Kicked the Hornets' Nest, Blomkvist risks his life researching the full extent of SÄPO's crimes, and persuades his sister Annika, a lawyer, to represent Salander, who has been cleared of the original murder suspicions, but is now charged with attempted murder and two cases of grievous bodily harm, as well as several other offences including possession of illegal weapons. With help from government prosecutors and Salander's fellow hackers, Blomkvist finds proof of the conspiracy and publishes an exposé article on the case, which results in several SÄPO agents being arrested. Using this information, Annika clears Salander's name. Blomkvist shows up at Salander's flat that night, and they reconcile as friends.
In the 2015 novel The Girl in the Spider's Web, written by David Lagercrantz as a continuation of the original series, Blomkvist again appears as one of the main protagonists. In the novel, Millennium's parent company, Serner Group, is trying to push Blomkvist out as editor. Desperate for a story, Blomkvist agrees to interview scientist Frans Balder about the theft of his quantum computer technology by hackers. When Balder is murdered, Blomkvist learns that he had hired Salander to hack his company, Solifon, to find out the thieves' identities. She had found out that a criminal organization called "The Spider Society" stole the data with help from Solifon employees and a mole in the National Security Agency. Salander enlists his help in protecting Balder's autistic son, August, from assassins working for the Spider Society, who had also murdered Balder.
Blomkvist meets Salander's sister, Camilla, and learns from Salander's former guardian, Holger Palmgren, that she is the leader of the Spider Society. When Camilla kills one of his reporters, Andrei Zander, Blomkvist—using information supplied by Salander—writes an article exposing Camilla's complicity with Solifon and the NSA in Balder's murder. The article nets Millennium enough money to buy out Serner, and re-establishes Blomkvist as one of Sweden's most respected journalists. The night the article is published, Blomkvist and Salander meet at his apartment.
Relationships[edit]
Blomkvist is divorced with one daughter – Pernilla – and throughout the trilogy has several lovers, including a brief affair with Lisbeth Salander. However, his primary partner throughout his adult life is Erika Berger, also his business partner. They enjoy an on-off sexual relationship which began years earlier before each married. Berger is still married and her husband knows about and accepts their open relationship. Towards the end of the first novel, Salander, after realising that she has fallen in love with him, and believing it to be one-sided, abruptly cuts off all contact with him. Blomkvist also has sexual relationships with three other characters in the series: Cecilia Vanger, Harriet Vanger and Monica Figuerola.
In film[edit]
In the 2009 Swedish version of The Girl with the Dragon Tattoo and its two sequels, Blomkvist is played by Michael Nyqvist. In the 2011 English adaptation, Blomkvist is played by Daniel Craig. In The Girl in the Spider's Web, he will be portrayed by Sverrir Gudnason.
References[edit]
Sweden portal
Fictional characters portal
Jump up ^ "Lisbeth Salander alias Pippi Longstocking, Astrid Lindgren". 20 January 2009. Archived from the original on 9 June 2009. Retrieved 27 September 2010.
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The Millennium series
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The Girl with the Dragon Tattoo
The Girl Who Played with Fire
The Girl Who Kicked the Hornets' Nest
David Lagercrantz
The Girl in the Spider's Web
The Girl Who Takes an Eye for an Eye
Films
Swedish films
The Girl with the Dragon Tattoo (2009)
The Girl Who Played with Fire (2009)
The Girl Who Kicked the Hornets' Nest (2009)
American films
The Girl with the Dragon Tattoo (2011) (soundtrack)
The Girl in the Spider's Web (2018)
Television
Millennium (2010)
Characters
Mikael Blomkvist
Lisbeth Salander
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Voltage-gated ion channel
From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Each of the four homologous domains makes up one subunit of the ion channel. The S4 voltage-sensing segments (marked with + symbols) are shown as charged.
Identifiers
Symbol
VIC
Pfam clan
CL0030
TCDB
1.A.1
OPM superfamily
8
OPM protein
2a79
Ions are depicted by the red circles. A gradient is represented by the different concentration of ions on either side of the membrane. The open conformation of the ion channel allows for the translocation of ions across the cell membrane, while the closed conformation does not.
Voltage-gated ion channels are a class of transmembrane proteins that form ion channels that are activated by changes in the electrical membrane potential near the channel. The membrane potential alters the conformation of the channel proteins, regulating their opening and closing. Cell membranes are generally impermeable to ions, thus they must diffuse through the membrane through transmembrane protein channels. They have a crucial role in excitable cells such as neuronal and muscle tissues, allowing a rapid and co-ordinated depolarization in response to triggering voltage change. Found along the axon and at the synapse, voltage-gated ion channels directionally propagate electrical signals. Voltage-gated ion-channels are usually ion-specific, and channels specific to sodium (Na+), potassium (K+), calcium (Ca2+), and chloride (Cl–) ions have been identified.[1] The opening and closing of the channels are triggered by changing ion concentration, and hence charge gradient, between the sides of the cell membrane.[2]
Contents
1 Structure
2 Mechanism
3 Different types
3.1 Sodium (Na+) channels
3.2 Calcium (Ca2+) channels
3.3 Potassium (K+) channels
3.4 Chloride (Cl−) channels
3.5 Proton (H+) channels
4 Phylogenetics
5 See also
6 References
7 External links
Structure[edit]
Further information: Cation channel superfamily
Conformation of the four homologous domains showing the formation of a central pore
Voltage-gated ion channels are generally composed of several subunits arranged in such a way that there is a central pore through which ions can travel down their electrochemical gradients. The channels tend to be ion-specific, although similarly sized and charged ions may sometimes travel through them. The functionality of voltage-gated ion channels is attributed to its three main discrete units: the voltage sensor, the pore or conducting pathway, and the gate.[3] Na+, K+, and Ca2+ channels are composed of four transmembrane domains arranged around a central pore; these four domains are part of a single α-subunit in the case of most Na+ and Ca2+ channels, whereas there are four α-subunits, each contributing one transmembrane domain, in most K+ channels.[4] The membrane-spanning segments, designated S1-S6, all take the form of alpha helices with specialized functions. The fifth and sixth transmembrane segments (S5 and S6) and pore loop serve the principal role of ion conduction, comprising the gate and pore of the channel, while S1-S4 serve as the voltage-sensing region.[3] The four subunits may be identical, or different from one another. In addition to the four central α-subunits, there are also regulatory β-subunits, with oxidoreductase activity, which are located on the inner surface of the cell membrane and do not cross the membrane, and which are coassembled with the α-subunits in the endoplasmic reticulum.[5]
Mechanism[edit]
Crystallographic structural studies of a potassium channel have shown that, when a potential difference is introduced over the membrane, the associated electric field induces a conformational change in the potassium channel. The conformational change distorts the shape of the channel proteins sufficiently such that the cavity, or channel, opens to allow influx or efflux to occur across the membrane. This movement of ions down their concentration gradients subsequently generates an electric current sufficient to depolarize the cell membrane.
Voltage-gated sodium channels and calcium channels are made up of a single polypeptide with four homologous domains. Each domain contains 6 membrane spanning alpha helices. One of these helices, S4, is the voltage sensing helix.[6] The S4 segment contains many positive charges such that a high positive charge outside the cell repels the helix, keeping the channel in its closed state.
In general, the voltage sensing portion of the ion channel is responsible for the detection of changes in transmembrane potential that trigger the opening or closing of the channel. The S1-4 alpha helices are generally thought to serve this role. In potassium and sodium channels, voltage-sensing S4 helices contain positively-charged lysine or arginine residues in repeated motifs.[3] In its resting state, half of each S4 helix is in contact with the cell cytosol. Upon depolarization, the positively-charged residues on the S4 domains move toward the exoplasmic surface of the membrane. It is thought that the first 4 arginines account for the gating current, moving toward the extracellular solvent upon channel activation in response to membrane depolarization. The movement of 10–12 of these protein-bound positive charges triggers a conformational change that opens the channel.[4] The exact mechanism by which this movement occurs is not currently agreed upon, however the canonical, transporter, paddle, and twisted models are examples of current theories.[7]
Movement of the voltage-sensor triggers a conformational change of the gate of the conducting pathway, controlling the flow of ions through the channel.[3]
The main functional part of the voltage-sensitive protein domain of these channels generally contains a region composed of S3b and S4 helices, known as the "paddle" due to its shape, which appears to be a conserved sequence, interchangeable across a wide variety of cells and species. A similar voltage sensor paddle has also been found in a family of voltage sensitive phosphatases in various species.[8] Genetic engineering of the paddle region from a species of volcano-dwelling archaebacteria into rat brain potassium channels results in a fully functional ion channel, as long as the whole intact paddle is replaced.[9] This "modularity" allows use of simple and inexpensive model systems to study the function of this region, its role in disease, and pharmaceutical control of its behavior rather than being limited to poorly characterized, expensive, and/or difficult to study preparations.[10]
Although voltage-gated ion channels are typically activated by membrane depolarization, some channels, such as inward-rectifier potassium ion channels, are activated instead by hyperpolarization.
The gate is thought to be coupled to the voltage sensing regions of the channels and appears to contain a mechanical obstruction to ion flow.[11] While the S6 domain has been agreed upon as the segment acting as this obstruction, its exact mechanism is unknown. Possible explanations include: the S6 segment makes a scissor-like movement allowing ions to flow through,[12] the S6 segment breaks into two segments allowing of passing of ions through the channel,[13] or the S6 channel serving as the gate itself.[14] The mechanism by which the movement of the S4 segment affects that of S6 is still unknown, however it is theorized that there is a S4-S5 linker whose movement allows the opening of S6.[3]
Inactivation of ion channels occurs within milliseconds after opening. Inactivation is thought to be mediated by an intracellular gate that controls the opening of the pore on the inside of the cell.[15] This gate is modeled as a ball tethered to a flexible chain. During inactivation, the chain folds in on itself and the ball blocks the flow of ions through the channel.[16] Fast inactivation is directly linked to the activation caused by intramembrane movements of the S4 segments,[17] though the mechanism linking movement of S4 and the engagement of the inactivation gate is unknown.
Different types[edit]
Sodium (Na+) channels[edit]
Sodium channels have similar functional properties across many different cell types. While ten human genes encoding for sodium channels have been identified, their function is typically conserved between species and different cell types.[17]
Calcium (Ca2+) channels[edit]
With sixteen different identified genes for human calcium channels, this type of channel differs in function between cell types. Ca2+ channels produce action potentials similarly to Na+ channels in some neurons. They also play a role in neurotransmitter release in pre-synaptic nerve endings. In most cells, Ca2+ channels regulate a wide variety of biochemical processes due to their role in controlling intracellular Ca2+ concentrations.[13]
Potassium (K+) channels[edit]
Potassium channels are the largest and most diverse class of voltage-gated channels, with over 100 encoding human genes. These types of channels differ significantly in their gating properties; some inactivating extremely slowly and others inactivating extremely quickly. This difference in activation time influences the duration and rate of action potential firing, which has a significant effect on electrical conduction along an axon as well as synaptic transmission. Potassium channels differ in structure from the other channels in that they contain four separate polypeptide subunits, while the other channels contain four homologous domain but on a single polypeptide unit.[7]
Chloride (Cl−) channels[edit]
Chloride channels are present in all types of neurons. With the chief responsibility of controlling excitability, chloride channels contribute to the maintenance of cell resting potential and help to regulate cell volume.[1]
Proton (H+) channels[edit]
Voltage-gated proton channels carry currents mediated by hydrogen ions in the form of hydronium, and are activated by depolarization in a pH-dependent manner. They function to remove acid from cells.[18][19][20]
Phylogenetics[edit]
Further information: Ion channel family
Phylogenetic studies of proteins expressed in bacteria revealed the existence of a superfamily of voltage-gated sodium channels.[21] Subsequent studies have shown that a variety of other ion channels and transporters are phylogenetically related to the voltage-gated ion channels, including inwardly rectifying K+ channels, ryanodine-inositol 1,4,5-triphosphate receptor Ca2+ channels, transient receptor potential Ca2+ channels, polycystin cation channels, glutamate-gated ion channels, calcium-dependent chloride channels, monovalent cation:proton antiporters, type 1, and potassium transporters.[22]
See also[edit]
Potassium channel
Catecholaminergic polymorphic ventricular tachycardia
References[edit]
^ Jump up to: a b Purves D, Augustine GJ, Fitzpatrick D, Katz LC, LaMantia A, McNamara JO, Williams SM (2001). "Voltage-Gated Ion Channels". Neuroscience (2nd ed.). Sunderland, Mass: Sinauer Associates. ISBN 978-0-87893-742-4.
Jump up ^ Catterall WA (April 2000). "From ionic currents to molecular mechanisms: the structure and function of voltage-gated sodium channels". Neuron. 26 (1): 13–25. doi:10.1016/S0896-6273(00)81133-2. PMID 10798388.
^ Jump up to: a b c d e Bezanilla F (March 2005). "Voltage-gated ion channels". IEEE Transactions on Nanobioscience. 4 (1): 34–48. doi:10.1109/tnb.2004.842463. PMID 15816170.
^ Jump up to: a b Lodish H, Berk A, Zipursky SL, Matsudaira P, Baltimore D, Darnell J (2000). "Section 21.3, Molecular Properties of Voltage-Gated Ion Channels". Molecular Cell Biology (4th ed.). New York: Scientific American Books. ISBN 978-0-7167-3136-8.
Jump up ^ Gulbis JM, Mann S, MacKinnon R (June 1999). "Structure of a voltage-dependent K+ channel beta subunit". Cell. 97 (7): 943–52. doi:10.1016/s0092-8674(00)80805-3. PMID 10399921.
Jump up ^ Catterall WA (2010). "Ion channel voltage sensors: structure, function, and pathophysiology". Neuron. 67 (6): 915–28. doi:10.1016/j.neuron.2010.08.021. PMC 2950829  . PMID 20869590.
^ Jump up to: a b Sands Z, Grottesi A, Sansom MS (2005). "Voltage-gated ion channels". Current Biology. 15 (2): R44–7. doi:10.1016/j.cub.2004.12.050. PMID 15668152.
Jump up ^ Murata Y, Iwasaki H, Sasaki M, Inaba K, Okamura Y (June 2005). "Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor". Nature. 435 (7046): 1239–43. Bibcode:2005Natur.435.1239M. doi:10.1038/nature03650. PMID 15902207.
Jump up ^ Alabi AA, Bahamonde MI, Jung HJ, Kim JI, Swartz KJ (November 2007). "Portability of paddle motif function and pharmacology in voltage sensors". Nature. 450 (7168): 370–5. Bibcode:2007Natur.450..370A. doi:10.1038/nature06266. PMC 2709416  . PMID 18004375.
Jump up ^ Long SB, Tao X, Campbell EB, MacKinnon R (November 2007). "Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment". Nature. 450 (7168): 376–82. Bibcode:2007Natur.450..376L. doi:10.1038/nature06265. PMID 18004376.
Jump up ^ Yellen G (August 1998). "The moving parts of voltage-gated ion channels". Quarterly Reviews of Biophysics. 31 (3): 239–95. doi:10.1017/s0033583598003448. PMID 10384687.
Jump up ^ Perozo E, Cortes DM, Cuello LG (July 1999). "Structural rearrangements underlying K+-channel activation gating". Science. 285 (5424): 73–8. doi:10.1126/science.285.5424.73. PMID 10390363.
^ Jump up to: a b Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R (May 2002). "Crystal structure and mechanism of a calcium-gated potassium channel". Nature. 417 (6888): 515–22. Bibcode:2002Natur.417..515J. doi:10.1038/417515a. PMID 12037559.
Jump up ^ Webster SM, Del Camino D, Dekker JP, Yellen G (April 2004). "Intracellular gate opening in Shaker K+ channels defined by high-affinity metal bridges". Nature. 428 (6985): 864–8. Bibcode:2004Natur.428..864W. doi:10.1038/nature02468. PMID 15103379.
Jump up ^ Armstrong CM (July 1981). "Sodium channels and gating currents". Physiological Reviews. 61 (3): 644–83. PMID 6265962.
Jump up ^ Vassilev P, Scheuer T, Catterall WA (October 1989). "Inhibition of inactivation of single sodium channels by a site-directed antibody". Proceedings of the National Academy of Sciences of the United States of America. 86 (20): 8147–51. Bibcode:1989PNAS...86.8147V. doi:10.1073/pnas.86.20.8147. PMC 298232  . PMID 2554301.
^ Jump up to: a b Bénitah JP, Chen Z, Balser JR, Tomaselli GF, Marbán E (March 1999). "Molecular dynamics of the sodium channel pore vary with gating: interactions between P-segment motions and inactivation". The Journal of Neuroscience. 19 (5): 1577–85. PMID 10024345.
Jump up ^ Cherny, V.V.; Markin, V.S.; DeCoursey, T.E. (1995), "The voltage-activated hydrogen ion conductance in rat alveolar epithelial cells is determined by the pH gradient" (PDF), Journal of General Physiology (published June 1995), 105 (6), pp. 861–896, doi:10.1085/jgp.105.6.861, retrieved 2008-07-14
Jump up ^ DeCoursey, T.E. (2003), "Voltage-gated proton channels and other proton transfer pathways", Physiological Reviews, 83 (2), pp. 475–579, doi:10.1152/physrev.00028.2002, OCLC 205658168, PMID 12663866, retrieved 2008-07-14
Jump up ^ Ramsey, I. Scott; Mokrab, Younes; Carvacho, Ingrid; Sands, Zara A.; Sansom, Mark S.P.; Clapham, David E. (2010). "An aqueous H+ permeation pathway in the voltage-gated proton channel Hv1". Nature Structural & Molecular Biology. 17 (7): 869–875. doi:10.1038/nsmb.1826. PMC 4035905  . PMID 20543828.
Jump up ^ Koishi R, Xu H, Ren D, Navarro B, Spiller BW, Shi Q, Clapham DE (March 2004). "A superfamily of voltage-gated sodium channels in bacteria". The Journal of Biological Chemistry. 279 (10): 9532–8. doi:10.1074/jbc.M313100200. PMID 14665618.
Jump up ^ Chang, Abraham B.; Lin, Ron; Studley, W. Keith; Tran, Can V.; Saier, Milton H., Jr. (2004). "Phylogeny as a guide to structure and function of membrane transport proteins". Mol Membr Biol. 21 (3): 171–181. doi:10.1080/09687680410001720830. PMID 15204625.
External links[edit]
IUPHAR-DB Voltage-gated ion channel subunits
The IUPHAR Compendium of Voltage-gated Ion Channels 2005
Voltage-Dependent+Anion+Channels at the US National Library of Medicine Medical Subject Headings (MeSH)
show
v
t
e
Membrane transport protein: ion channels (TC 1A)
show
Ca2+: Calcium channel
Ligand-gated
Inositol trisphosphate receptor
1
2
3
Ryanodine receptor
1
2
3
Voltage-gated
L-type/Cavα
1.1
1.2
1.3
1.4
N-type/Cavα2.2
P-type/Cavα
2.1
Q-type/Cavα2.1
R-type/Cavα2.3
T-type/Cavα
3.1
3.2
3.3
α2δ-subunits
1
2
β-subunits
β1
β2
β3
β4
γ-subunits
γ1
γ2
γ3
γ4
Cation channels of sperm
1
2
3
4
Two-pore channel
1
2
show
Na+: Sodium channel
Constitutively active
Epithelial sodium channel
α
β
γ
δ
Proton-gated
Amiloride-sensitive cation channel
1
2
3
4
Voltage-gated
Navα
1.1
1.2
1.3
1.4
1.5
1.6
1.7
1.8
1.9
7A
Navβ
1
2
3
4
show
K+: Potassium channel
Calcium-activated
BK channel
α1
β1
β2
β3
β4
SK channel
SK1
SK2
SK3
IK channel
IK1
KCa
1.1
2.1
2.2
2.3
3.1
4.1
4.2
5.1
Inward-rectifier
KATP
Kir
1.1
2.1
2.2
2.3
2.4
2.6
GIRK/Kir
3.1
3.2
3.3
3.4
Kir
4.1
4.2
5.1
6.1
6.2
7.1
Tandem pore domain
K2P
1
2
3
4
5
6
7
9
10
12
13
15
16
17
18
Voltage-gated
Kvα1-6
1.1
1.2
1.3
1.4
1.5
1.6
1.7
1.8
2.1
2.2
3.1
3.2
3.3
3.4
4.1
4.2
4.3
5.1
6.1
6.2
6.3
6.4
Kvα7-12
7.1
7.2
7.3
7.4
7.5
8.1
8.2
9.1
9.2
9.3
10.1
10.2
11.1/hERG
11.2
11.3
12.1
12.2
12.3
Kvβ
1
2
3
KCNIP
1
2
3
4
minK/ISK
minK/ISK-like
MiRP
1
2
3
Shaker gene
show
Miscellaneous
Cl−: Chloride channel
Calcium-activated chloride channels
Anoctamin
ANO1
Bestrophin
1
2
Chloride Channel Accessory
1
2
3
4
CFTR
CLCN
1
2
3
4
5
6
7
KA
KB
CLIC
1
2
3
4
5
6
L1
CLNS
1A
1B
H+: Proton channel
HVCN1
M+: CNG cation channel
α
1
2
3
4
β
1
2
3
HCN
FC
1
2
3
4
M+: TRP cation channel
TRPA (1)
TRPC
1
2
3
4
4AP
5
6
7
TRPM
1
2
3
4
5
6
7
8
TRPML
1
2
3
TRPN
TRPP
1
2
TRPV
1
2
3
4
5
6
H2O (+ solutes): Porin
Aquaporin
0
1
2
3
4
5
6
7
8
9
Voltage-dependent anion channel
1
2
3
General bacterial porin family
Cytoplasm: Gap junction
Connexin
A
GJA1
GJA3
GJA4
GJA5
GJA8
GJA9
GJA10
B
GJB1
GJB2
GJB3
GJB4
GJB5
GJB6
GJB7
C
GJC1
GJC2
GJC3
D
GJD2
GJD3
GJD4
Innexin
hide
By gating mechanism
Ion channel class
Ligand-gated
Light-gated
Voltage-gated
Stretch-activated
see also disorders
Retrieved from "https://en.wikipedia.org/w/index.php?title=Voltage-gated_ion_channel&oldid=838977333"
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