Cytoplasmic FMR1-interacting protein 2 is a protein that in humans is encoded by the CYFIP2 gene. [5] [6] Cytoplasmic FMR1 interacting protein is a 1253 amino acid long protein and is highly conserved sharing 99% sequence identity to the mouse protein. [5] [7] It is expressed mainly in brain tissues, white blood cells and the kidney. [8]
CYFIP2 has been shown to interact with FMR1. [5] [9] CYFIP2 is a p-53 inducible protein [10] and also interacts with the Fragile=X mental retardation protein. [11]
The pre-mRNA of this protein is subject to RNA editing. [12] The editing site was previously recorded as a single nucleotide polymorphism (rs3207362) in the dbSNP. [12]
A to I RNA editing is catalyzed by a family of adenosine deaminases acting on RNA (ADARs) that specifically recognize adenosines within double-stranded regions of pre-mRNAs and deaminate them to inosine. Inosines are recognised as guanosine by the cells translational machinery. There are three members of the ADAR family ADARs 1-3 with ADAR1 and ADAR2 being the only enzymatically active members. ADAR3 is thought to have a regulatory role in the brain. ADAR1 and ADAR 2 are widely expressed in tissues while ADAR3 is restricted to the brain. The double stranded regions of RNA are formed by base-pairing between residues in the close to region of the editing site with residues usually in a neighboring intron but can be an exonic sequence. The region that base pairs with the editing region is known as an Editing Complementary Sequence (ECS).
An editing site was found in the pre-mRNA of this protein. The substitution occurs within amino acid position 320 in humans and also in mice. A possible double stranded RNA region has not been detected for this pre-mRNA. [12] No double stranded region required by ADARs has predicted. Immunoprecipitation experiments and RNA interference have shown that ADAR 2 is likely to be the main editing enzyme for this site with ADAR 1 having a minor role. [13] [14]
Editing seems to be differentially regulated in different tissues. The highest level of editing occurs in the cerebellum with lower frequency of editing detected in human lung, prostrate and uterus tissues. Editing frequency varies from 30-85% depending on tissue. [12] [13] { [14] There is some evidence for a decrease in CYFIP2 editing with increased age. [15]
Editing of the pre-mRNA of this gene has been detected in mouse and chicken. [12]
Editing results in a codon change resulting in a glutamic acid being translated instead of a lysine. [12]
Currently unknown but editing may have role in regulation of apoptotic functions of this protein. It is thought that since the protein is p53 inducible that the protein may be pro-apopototic. Also ADAR1 knock out mice show increase in apoptosis which indicates editing may be involved in regulation of the cellular process. [10] [12]
Z-DNA is one of the many possible double helical structures of DNA. It is a left-handed double helical structure in which the helix winds to the left in a zigzag pattern, instead of to the right, like the more common B-DNA form. Z-DNA is thought to be one of three biologically active double-helical structures along with A-DNA and B-DNA.
FMR1 is a human gene that codes for a protein called fragile X messenger ribonucleoprotein, or FMRP. This protein, most commonly found in the brain, is essential for normal cognitive development and female reproductive function. Mutations of this gene can lead to fragile X syndrome, intellectual disability, premature ovarian failure, autism, Parkinson's disease, developmental delays and other cognitive deficits. The FMR1 premutation is associated with a wide spectrum of clinical phenotypes that affect more than two million people worldwide.
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. Isaacs syndrome is a result of an autoimmune reaction against the Kv1.1 ion channel.
Missense mRNA is a messenger RNA bearing one or more mutated codons that yield polypeptides with an amino acid sequence different from the wild-type or naturally occurring polypeptide. Missense mRNA molecules are created when template DNA strands or the mRNA strands themselves undergo a missense mutation in which a protein coding sequence is mutated and an altered amino acid sequence is coded for.
Glutamate receptor 3 is a protein that in humans is encoded by the GRIA3 gene.
Filamin A, alpha (FLNA) is a protein that in humans is encoded by the FLNA gene.
The double-stranded RNA-specific adenosine deaminase enzyme family are encoded by the ADAR family genes. ADAR stands for adenosine deaminase acting on RNA. This article focuses on the ADAR proteins; This article details the evolutionary history, structure, function, mechanisms and importance of all proteins within this family.
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 low affinity compared to IGFBPs 1-6. It also stimulates cell adhesion. The protein is implicated in some cancers.
Fragile X mental retardation syndrome-related protein 1 is a protein that in humans is encoded by the FXR1 gene.
Glutamate receptor, ionotropic, kainate 1, also known as GRIK1, is a protein that in humans is encoded by the GRIK1 gene.
Fragile X mental retardation syndrome-related protein 2 is a protein that in humans is encoded by the FXR2 gene.
Gamma-aminobutyric acid receptor subunit alpha-3 is a protein that in humans is encoded by the GABRA3 gene.
Cytoplasmic FMR1-interacting protein 1 is a protein that in humans is encoded by the CYFIP1 gene.
Nuclear fragile X mental retardation-interacting protein 2 is a protein that in humans is encoded by the NUFIP2 gene.
Bladder cancer-associated protein is a protein that in humans is encoded by the BLCAP gene.
Nuclear fragile X mental retardation-interacting protein 1 is a protein that in humans is encoded by the NUFIP1 gene.
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.
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.
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 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 efficiencies of up to 80%.
