Introduction of CACNA1F
CACNA1F, voltage-dependent, L type alpha 1F subunit, also known as Cav1.4, is a protein that in human is encoded by CACNA1F gene. It is a member of the alpha-1 subunit family, and it’s one of the proteins involved in the voltage-dependent calcium channel complex. CACNA1F mediates the calcium influx into the cell once membrane polarization. In addition, CACNA1F is a complex which consists of alpha-1, alpha-2/delta, beta, and gamma subunits as a 1 to 1 to 1 to 1 ratio. The alpha-1 subunit includes 24 transmembrane segments and forms the pore by which ions pass into the cell. Multiple isoforms of each protein in the complex are available, either encoded by different genes or the result of alternative splicing of transcripts.
|Basic Information of CACNA1F|
|Protein Name||Voltage-dependent L-type calcium channel subunit alpha-1F|
|Aliases||Voltage-gated calcium channel subunit alpha Cav1.4, CACNAF1|
|Organism||Homo sapiens (Human)|
Function of CACNA1F Membrane Protein
CACNA1F, calcium channel is a voltage-dependent, L-type calcium channel subunit alpha-1F. Mediating the entry of calcium ions into excitable cells, voltage-sensitive calcium channels (VSCC) are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1F can cause L-type calcium currents. Researchers have reported that long-lasting (L-type) calcium channels are members of the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), benzothiazepines, as well as phenylalkylamines and omega-agatoxin-IIIA (omega-Aga-IIIA). CACNA1F is insensitive to omega-agatoxin-IVA (omega-Aga-IVA), as well as omega-conotoxin-GVIA (omega-CTx-GVIA). Furthermore, CACNA1F is also activated at more negative voltages and does not process calcium-dependent inactivation (CDI), due to incoming calcium ions during depolarization.
Fig.1 Protein topology of Cav1.4. (Waldner, 2018)
Application of CACNA1F Membrane Protein in Literature
This article addresses the special properties of one L-type VGCC, Cav1.4, with particular emphasis on its role in the transmission of visual signals from rod and cone photoreceptors to the second-order retinal neurons, and the pathological effects of mutations in the CACNA1F gene which codes for the pore-forming α1F subunit of Cav1.4.
This article is to describe in detail cases with an initial diagnosis of Leber congenital amaurosis that is later found to have a hemizygous mutation in the CACNA1F gene.
This study shows that genetic deletion of the synaptic Cav1.4 L-type VGCCs impairs calpain activation and leads to a short-term preservation of photoreceptors in the rd1 mouse.
This article concludes that exon 47 encodes structural determinants that regulate CDI and voltage-dependent activation of Cav1.4, and is necessary for modulation of channel activation by CaBP4.
This article shows that a key function of RIM1/2 at rod ribbons is to enhance Cav1.4 channel activity, possibly through direct or indirect modulation of the channel.
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