NARF
From Wikipedia, the free encyclopedia
Nuclear prelamin A recognition factor, also known as NARF, is a protein which in humans is encoded by the NARF gene.[1][2][3]
[edit] Function
Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing.[1]
[edit] Interactions
NARF has been shown to interact with LMNA.[2]
[edit] References
[edit] Further reading
- Maltese WA (1991). "Posttranslational modification of proteins by isoprenoids in mammalian cells". FASEB J. 4 (15): 3319–28. PMID 2123808.
- Barton RM, Worman HJ (1999). "Prenylated prelamin A interacts with Narf, a novel nuclear protein". J. Biol. Chem. 274 (42): 30008–18. doi:10.1074/jbc.274.42.30008. PMID 10514485.
- Strausberg RL, Feingold EA, Grouse LH et al (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Ota T, Suzuki Y, Nishikawa T et al (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Hackstein JH (2005). "Eukaryotic Fe-hydrogenases -- old eukaryotic heritage or adaptive acquisitions?". Biochem. Soc. Trans. 33 (Pt 1): 47–50. doi:10.1042/BST0330047. PMID 15667261.
- Rual JF, Venkatesan K, Hao T et al (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Kimura K, Wakamatsu A, Suzuki Y et al (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.
- Yamada M, Ohnishi J, Ohkawara B et al (2006). "NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF)". J. Biol. Chem. 281 (30): 20749–60. doi:10.1074/jbc.M602089200. PMID 16714285.
- Lev-Maor G, Sorek R, Levanon EY et al (2007). "RNA-editing-mediated exon evolution". Genome Biol. 8 (2): R29. doi:10.1186/gb-2007-8-2-r29. PMC 1852406. PMID 17326827. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1852406.
