Regulation of CaV1.2 Current: Interaction With Intracellular Molecules
| Autor: | Mitsuhiro Fukao, Yoichi Yamada, Masaaki Tsutsuura, Takeshi Kobayashi, Noritsugu Tohse |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Pharmacology
Calmodulin biology Calcium Channels L-Type Sequence Homology Amino Acid Protein subunit PDZ domain Calcium-Binding Proteins Molecular Sequence Data lcsh:RM1-950 N-type calcium channel Cav1.2 Cell biology Membrane Potentials R-type calcium channel lcsh:Therapeutics. Pharmacology Ca2+/calmodulin-dependent protein kinase biology.protein Molecular Medicine Animals Humans Amino Acid Sequence ATP synthase alpha/beta subunits Protein Binding Signal Transduction |
| Zdroj: | Journal of Pharmacological Sciences, Vol 103, Iss 4, Pp 347-353 (2007) |
| ISSN: | 1347-8613 |
| Popis: | Ca(V)1.2 (alpha(1c)) is a pore-forming subunit of the voltage-dependent L-type calcium channel and is expressed in many tissues. The beta and alpha(2)/delta subunits are auxiliary subunits that affect the kinetics and the expression of Ca(V)1.2. In addition to the beta and alpha(2)/delta subunits, several molecules have been reported to be involved in the regulation of Ca(V)1.2 current. Calmodulin, CaBP1 (calcium-binding protein-1), CaMKII (calcium/calmodulin-dependent protein kinase II), AKAPs (A-kinase anchoring proteins), phosphatases, Caveolin-3, beta(2)-adrenergic receptor, PDZ domain proteins, sorcin, SNARE proteins, synaptotagmin, CSN5, RGK family, and AHNAK1 have all been reported to interact with Ca(V)1.2 and the beta subunit. This review focuses on the effect of these molecules on Ca(V)1.2 current. |
| Databáze: | OpenAIRE |
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