Potassium channel RNA editing signal

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Potassium channel RNA editing signal
RF00485.jpg
Predicted secondary structure and sequence conservation of K_chan_RES
Identifiers
SymbolK_chan_RES
Rfam RF00485
Other data
RNA type Cis-reg
Domain(s) Eukaryota
SO SO:0000233
PDB structures PDBe

The potassium channel RNA editing signal is an RNA element found in human Kv1.1 and its homologues which directs the efficient modification of an adenosine to inosine by an adenosine deaminase acting on RNA (ADAR). The ADAR modification causes an isoleucine/valine recoding event which lies in the ion-conducting pore of the potassium channel. It is thought that this editing event targets the process of fast inactivation and allows a more rapid recovery from inactivation at negative potentials. [1]

Related Research Articles

RNA editing

RNA editing is a molecular process through which some cells can make discrete changes to specific nucleotide sequences within an RNA molecule after it has been generated by RNA polymerase. It occurs in all living organisms, and is one of the most evolutionarily conserved properties of RNAs. RNA editing may include the insertion, deletion, and base substitution of nucleotides within the RNA molecule. RNA editing is relatively rare, with common forms of RNA processing not usually considered as editing. It can affect the activity, localization as well as stability of RNAs, and has been linked with human diseases.

Kv1.1

Potassium voltage-gated channel subfamily A member 1 also known as Kv1.1 is a shaker related voltage-gated potassium channel that in humans is encoded by the KCNA1 gene. The Isaacs syndrome is a result of an autoimmune reaction against the Kv1.1 ion channel.

GRIA3

Glutamate receptor 3 is a protein that in humans is encoded by the GRIA3 gene.

FLNA

Filamin A, alpha (FLNA) is a protein that in humans is encoded by the FLNA gene.

ADAR

Double-stranded RNA-specific adenosine deaminase is an enzyme that in humans is encoded by the ADAR gene.

GRIA2

Glutamate ionotropic receptor AMPA type subunit 2 is a protein that in humans is encoded by the GRIA2 gene.

GRIK2

Glutamate ionotropic receptor kainate type subunit 2, also known as ionotropic glutamate receptor 6 or GluR6, is a protein that in humans is encoded by the GRIK2 gene.

IGFBP7

Insulin-like growth factor-binding protein 7 is a protein that in humans is encoded by the IGFBP7 gene. The major function of the protein is the regulation of availability of insulin-like growth factors (IGFs) in tissue as well as in modulating IGF binding to its receptors. IGFBP7 binds to IGF with high affinity. It also stimulates cell adhesion. The protein is implicated in some cancers.

ADARB1

Double-stranded RNA-specific editase 1 is an enzyme that in humans is encoded by the ADARB1 gene.

GRIK1

Glutamate receptor, ionotropic, kainate 1, also known as GRIK1, is a protein that in humans is encoded by the GRIK1 gene.

CYFIP2

Cytoplasmic FMR1-interacting protein 2 is a protein that in humans is encoded by the CYFIP2 gene. Cytoplasmic FMR1 interacting protein is a 1253 amino acid long protein and is highly conserved sharing 99% sequence identity to the mouse protein. It is expressed mainly in brain tissues, white blood cells and the kidney.

GRIA4

Glutamate receptor 4 is a protein that in humans is encoded by the GRIA4 gene.

GABRA3

Gamma-aminobutyric acid receptor subunit alpha-3 is a protein that in humans is encoded by the GABRA3 gene.

BLCAP

Bladder cancer-associated protein is a protein that in humans is encoded by the BLCAP gene.

ADARB2

Double-stranded RNA-specific editase B2 is an enzyme that in humans is encoded by the ADARB2 gene.

ARL6IP4

ADP-ribosylation-like factor 6 interacting protein 4 (ARL6IP4), also called SRp25 is the product of the ARL6IP4 gene located on chromosome 12q24. 31. Its function is unknown.

In human genetics, the GRIA2 gene is located on chromosome 4q32-q33. The gene product is the ionotropic AMPA glutamate receptor 2. The protein belongs to a family of ligand-activated glutamate receptors that are sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA). Glutamate receptors function as the main excitatory neurotransmitter at many synapses in the central nervous system. L-glutamate, an excitatory neurotransmitter, binds to the Gria2 resulting in a conformational change. This leads to the opening of the channel converting the chemical signal to an electrical impulse. AMPA receptors (AMPAR) are composed of four subunits, designated as GluR1 (GRIA1), GluR2 (GRIA2), GluR3 (GRIA3), and GluR4(GRIA4) which combine to form tetramers. They are usually heterotrimeric but can be homodimeric. Each AMPAR has four sites to which an agonist can bind, one for each subunit.[5]

C1QL1

The complement component 1, q subcomponent-like 1 is encoded by a gene located at chromosome 17q21.31. It is a secreted protein and is 258 amino acids in length. The protein is widely expressed but its expression is highest in the brain and may also be involved in regulation of motor control. The pre-mRNA of this protein is subject to RNA editing.

Adenosine deaminase z-alpha domain

In molecular biology, the protein domain Adenosine deaminase z-alpha domain refers to an evolutionary conserved protein domain. This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA-editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.

LEAPER gene editing Gene editing method

LEAPER is a genetic engineering technique in molecular biology by which RNA can be edited. The technique relies on engineered strands of RNA to recruit native ADAR enzymes to swap out different compounds in RNA. Developed by researchers at Peking University in 2019, the technique, some have claimed, is more efficient than the CRISPR gene editing technique. Initial studies have claimed that editing efiiciencies of up to 80% can be achieved.

References

  1. Bhalla T, Rosenthal JJ, Holmgren M, Reenan R (October 2004). "Control of human potassium channel inactivation by editing of a small mRNA hairpin". Nature Structural & Molecular Biology. 11 (10): 950–956. doi:10.1038/nsmb825. PMID   15361858. S2CID   34081059.