CACNA1F Membrane Protein Introduction

Introduction of CACNA1F

CACNA1F, voltage-dependent, L type alpha 1F subunit, also known as Ca_v1.4, 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.

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 Ca_v1.4. (Waldner, 2018)

Application of CACNA1F Membrane Protein in Literature

1. Waldner D.M., et al. Channeling Vision: Ca_v1.4-A Critical Link in Retinal Signal Transmission. Biomed Res Int. 2018, 2018: 7272630. PubMed ID: 29854783
   
   

   This article addresses the special properties of one L-type VGCC, Ca_v1.4, 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 Ca_v1.4.

2. Men C.J., et al. The importance of genetic testing as demonstrated by two cases of CACNA1F-associated retinal generation misdiagnosed as LCA. Mol Vis. 2017, 23: 695-706. PubMed ID: 29062221
   
   

   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.

3. Schön C., et al. Ca_v1.4 L-Type Calcium Channels Contribute to Calpain Activation in Degenerating Photoreceptors of rd1 Mice. PLoS One. 2016, 11(6): e0156974. PubMed ID: 27270916
   
   

   This study shows that genetic deletion of the synaptic Ca_v1.4 L-type VGCCs impairs calpain activation and leads to a short-term preservation of photoreceptors in the rd1 mouse.

4. Haeseleer F., et al. Characterization of C-terminal Splice Variants of Ca_v1.4 Ca²⁺ Channels in Human Retina. J Biol Chem. 2016, 291(30): 15663-73. PubMed ID: 27226626
   
   

   This article concludes that exon 47 encodes structural determinants that regulate CDI and voltage-dependent activation of Ca_v1.4, and is necessary for modulation of channel activation by CaBP4.

5. Grabner C.P., et al. RIM1/2-Mediated Facilitation of Ca_v1.4 Channel Opening Is Required for Ca²⁺-Stimulated Release in Mouse Rod Photoreceptors. J Neurosci. 2015, 35(38): 13133-47. PubMed ID: 26400943
   
   

   This article shows that a key function of RIM1/2 at rod ribbons is to enhance Ca_v1.4 channel activity, possibly through direct or indirect modulation of the channel.

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Reference

1. Waldner D M, et al. (2018). Channeling Vision: Ca_v1.4-A Critical Link in Retinal Signal Transmission. Biomed Res Int. 2018:7272630.

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