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- W4211244655 abstract "Abstract High‐voltage‐activated calcium channels (Ca V 1s and Ca V 2s) are transmembrane protein complexes that couple membrane depolarization to cellular calcium entry. Because calcium is an intracellular messenger and Ca V s are important calcium sources, Ca V s have a key role in the conversion of electrical signals into the chemical signaling cascades that drive a variety of vital physiological processes in nerve and muscle. These include excitation‐contraction coupling, hormone release, gene regulation, and synaptic transmission. Ca V s are regulated by a diverse set of feedback mechanisms. Two important forms of activity‐dependent feedback modulation involve interactions between calcium‐calmodulin (Ca 2+ /CaM) and the Ca V α 1 pore‐forming subunit of Ca V 1s and Ca V 2s: calcium‐dependent inactivation (CDI) in which calcium influx promotes channel closing following activation, and calcium‐dependent facilitation (CDF), a process that enhances channel opening in response to elevated cytoplasmic calcium. The main site of action for Ca 2+ /CaM is a motif, known as an IQ domain , located on the C‐terminal cytoplasmic tail of the Ca V α 1 pore‐forming subunit. Strikingly, different Ca 2+ /CaM lobes are responsible for CDI and CDF in Ca V 1 and Ca V 2 channels. Crystallographic studies have indicated a structural basis for the apparent inversion of lobe‐specific roles in CDI and CDF in which Ca 2+ /CaM binds Ca V 1 and Ca V 2 IQ domains in opposite orientations." @default.
- W4211244655 created "2022-02-13" @default.
- W4211244655 creator A5032711040 @default.
- W4211244655 creator A5045437602 @default.
- W4211244655 creator A5075337100 @default.
- W4211244655 date "2004-03-05" @default.
- W4211244655 modified "2023-09-26" @default.
- W4211244655 title "Calmodulin Interactions with <scp>C</scp> a <sub>v</sub> 1 and <scp>C</scp> a <sub>v</sub> 2 Voltage‐Gated Calcium Channel <scp>IQ</scp> Domains" @default.
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