KCND tetramer:KCNIP tetramer transport K+ from cytosol to extracellular region

Stable Identifier
R-HSA-5577234
Type
Reaction [transition]
Species
Homo sapiens
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In phase 1 of the action potential, the fast Na+ channels are inactivated. This happens by net outward currents Ito1 and Ito2 caused by efflux of K+ and Cl- ions respectively. Potassium voltage-gated channel subfamily D members 1, 2 and 3 (KCND1, 2 and 3) are pore-forming (alpha) subunits of voltage-gated, rapidly inactivating A-type K+ channels (Isbrandt et al. 2000) that produce the Ito1 current. They may also contribute to the ISa current in neurons. KCND1 is functional as either a homo- or hetero-tetramer with KCND2 and/or KCND3. KCNDs associate with the regulatory subunits KCNIP1-4 (Scannevin et al. 2004, Pioletti et al. 2006). KCNIPs form homodimers and/or homotetramers (Lin et al. 2004). KCNIPs and KCNDs together modulate the density, inactivation kinetics and rate of recovery from inactivation of KCNDs (An et al. 2000, Nakamura et al. 2001, Shibata et al. 2003, Wang et al. 2007).

Literature References
PubMed ID Title Journal Year
17187064 Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits

Wang, H, Yan, Y, Liu, Q, Huang, Y, Shen, Y, Chen, L, Chen, Y, Yang, Q, Hao, Q, Wang, K, Chai, J

Nat. Neurosci. 2007
10729221 Gene structures and expression profiles of three human KCND (Kv4) potassium channels mediating A-type currents I(TO) and I(SA)

Isbrandt, D, Leicher, T, Waldschütz, R, Zhu, X, Luhmann, U, Michel, U, Sauter, K, Pongs, O

Genomics 2000
15358149 Protein-protein interactions of KChIP proteins and Kv4.2

Lin, YL, Chen, CY, Cheng, CP, Chang, LS

Biochem. Biophys. Res. Commun. 2004
14980207 Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1

Scannevin, RH, Wang, K, Jow, F, Megules, J, Kopsco, DC, Edris, W, Carroll, KC, Lü, Q, Xu, W, Xu, Z, Katz, AH, Olland, S, Lin, L, Taylor, M, Stahl, M, Malakian, K, Somers, W, Mosyak, L, Bowlby, MR, Chanda, P, Rhodes, KJ

Neuron 2004
17057713 Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer

Pioletti, M, Findeisen, F, Hura, GL, Minor, DL

Nat. Struct. Mol. Biol. 2006
11423117 Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4 subfamily members, Kv4.1 and Kv4.2

Nakamura, TY, Nandi, S, Pountney, DJ, Artman, M, Rudy, B, Coetzee, WA

FEBS Lett. 2001
10676964 Modulation of A-type potassium channels by a family of calcium sensors

An, WF, Bowlby, MR, Betty, M, Cao, J, Ling, HP, Mendoza, G, Hinson, JW, Mattsson, KI, Strassle, BW, Trimmer, JS, Rhodes, KJ

Nature 2000
12829703 A fundamental role for KChIPs in determining the molecular properties and trafficking of Kv4.2 potassium channels

Shibata, R, Misonou, H, Campomanes, CR, Anderson, AE, Schrader, LA, Doliveira, LC, Carroll, KI, Sweatt, JD, Rhodes, KJ, Trimmer, JS

J. Biol. Chem. 2003
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Title
A-type (transient outward) potassium channel activity of KCND tetramer:KCNIP tetramer [plasma membrane]
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