K+ voltage-gated channel subfamily B member 1; delayed rectifier K+ channel 1; DRK1; h-DRK1; voltage-gated K+ channel subunit Kv2.1 (KCNB1)
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Function
- mediates voltage-dependent K+ permeability of excitable membranes
- channels open or close in response to the voltage difference across the membrane, letting K+ pass in accordance with their electrochemical gradient
- highly phosphorylated on Ser in the C-terminal
- differential phosphorylation on a subset of Ser allows graded activity-dependent regulation of channel gating
- phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-656 & Ser-720 as well as the N-terminal Ser-15 are all regulated by calcineurin-mediated dephosphorylation
- particularly, Ser-607 & Tyr-128 are significant sites of voltage-gated regulation through phosphorylation - dephosphorylation activities
- Tyr-128 can be dephosphorylated by PTpalpha & cyt-PTpepsilon
- phosphorylation levels on Ser-607 are supersensitive to neuronal activity
- phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 & P5
- levels then increase to reach adult levels by P14
- phosphorylation levels on Ser-564 & Ser-607 are greatly reduced during seizures, by 40% & 85% respectively
- heteromultimer with KCNG2, KCNG3, KCNG4, KCNS1, KCNS2, KCNS3 & KCNV2 (putative)
Structure
- the segment S4 is probably the voltage-sensor & is characterized by a series of positively charged amino acids at every third position
- the tail may be important in modulation of channel activity &/or targeting of the channel to specific subcellular compartments
- belongs to the K+ channel family, B (Shab) (TC 1.A.1.2) subfamily, Kv2.1/KCNB1 sub-subfamily
Compartment
membrane