Developer site: The content shown here is test data.

MyEClinic
MyEClinic
Health Dictionary AI Health Chat Find an Online Doctor
A serene Zen garden with raked sand and smooth stones, symbolising clarity and calm

Health Dictionary

Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

Back to skin conditions

CYFIP2

Introduction

Cytoplasmic FMR1-interacting protein 2 is a protein that in humans is encoded by the CYFIP2 gene.[1][2] Cytoplasmic FMR1 interacting protein is a 1253 amino acid long protein and is highly conserved sharing 99% sequence identity to the mouse protein.[1][3] It is expressed mainly in brain tissues, white blood cells and the kidney.[4]

Interactions

Interactions

CYFIP2 has been shown to interact with FMR1.[1][5] CYFIP2 is a p-53 inducible protein[6] and also interacts with the Fragile=X mental retardation protein.[7]

RNA editing

RNA editing

The pre-mRNA of this protein is subject to RNA editing.[8] The editing site was previously recorded as a single nucleotide polymorphism (rs3207362) in the dbSNP.[8]

Type

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).

Site

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.[8] 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.[9][10]

Regulation

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.[8][9]{[10] There is some evidence for a decrease in CYFIP2 editing with increased age.[11]

Conservation

Editing of the pre-mRNA of this gene has been detected in mouse and chicken.[8]

Effects of RNA editing

Structural

Editing results in a codon change resulting in a glutamic acid being translated instead of a lysine.[8]

Functional

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.[6][8]

References

References

  1. ↑ 1.0 1.1 1.2 Schenck A, Bardoni B, Moro A, Bagni C, Mandel JL (Jul 2001). “A highly conserved protein family interacting with the fragile X genetic condition protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P”. Proc Natl Acad Sci U S A. 98 (15): 8844–9. doi:10.1073/pnas.151231598. PMC 37523. PMID 11438699.
  2. ↑ “Entrez Gene: CYFIP2 cytoplasmic FMR1 interacting protein 2”.
  3. ↑ https://www.genecards.org/cgi-bin/carddisp.pl?gene=GRIA4
  4. ↑ Su AI, Wiltshire T, Batalov S, et al. (April 2004). “A gene atlas of the mouse and human protein-encoding transcriptomes”. Proc. Natl. Acad. Sci. U.S.A. 101 (16): 6062–7. doi:10.1073/pnas.0400782101. PMC 395923. PMID 15075390.
  5. ↑ Bardoni B, Castets M, Huot ME, Schenck A, Adinolfi S, Corbin F, Pastore A, Khandjian EW, Mandel JL (July 2003). “82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization”. Hum. Mol. Genet. 12 (14): 1689–98. doi:10.1093/hmg/ddg181. PMID 12837692.
  6. ↑ 6.0 6.1 Saller E, Tom E, Brunori M, et al. (August 1999). “Increased apoptosis induction by 121F mutant p53”. EMBO J. 18 (16): 4424–37. doi:10.1093/emboj/18.16.4424. PMC 1171517. PMID 10449408.
  7. ↑ Schenck, A., Bardoni, B., Moro, A., Bagni, C., Mandel, J.-L. (2001) Proceedings of the National Academy of Sciences of the United States of America, 98, 8844-8849.
  8. ↑ 8.0 8.1 8.2 8.3 8.4 8.5 8.6 Levanon EY, Hallegger M, Kinar Y, Shemesh R, Djinovic-Carugo K, Rechavi G, Jantsch MF, Eisenberg E (2005). “Evolutionarily conserved human targets of adenosine to inosine RNA editing”. Nucleic Acids Res. 33 (4): 1162–8. doi:10.1093/nar/gki239. PMC 549564. PMID 15731336.
  9. ↑ 9.0 9.1 Riedmann EM, Schopoff S, Hartner JC, Jantsch MF (June 2008). “Specificity of ADAR-mediated RNA editing in newly identified targets”. RNA. 14 (6): 1110–8. doi:10.1261/rna.923308. PMC 2390793. PMID 18430892.
  10. ↑ 10.0 10.1 Nishimoto Y, Yamashita T, Hideyama T, Tsuji S, Suzuki N, Kwak S (June 2008). “Determination of editors at the novel A-to-I editing positions”. Neurosci. Res. 61 (2): 201–6. doi:10.1016/j.neures.2008.02.009. PMID 18407364.
  11. ↑ Nicholas A, de Magalhaes JP, Kraytsberg Y, Richfield EK, Levanon EY, Khrapko K (June 2010). “Age-related gene-specific changes of A-to-I mRNA editing in the human brain”. Mech. Ageing Dev. 131 (6): 445–7. doi:10.1016/j.mad.2010.06.001. PMC 2915444. PMID 20538013.
External links
Further reading

Further reading