Interleukin enhancer-binding factor 2

Definition:

Chromatin-interacting protein that forms a stable heterodimer with interleukin enhancer-binding factor 3/ILF3 and plays a role in several biological processes including transcription, innate immunity or cell growth. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. Together with ILF3, forms an RNA-binding complex that is required for mitotic progression and cytokinesis by regulating the expression of a cluster of mitotic genes. Mechanistically, competes with STAU1/STAU2-mediated mRNA decay. Also plays a role in the inhibition of various viruses including Japanese encephalitis virus or enterovirus 71.; (Microbial infection) Plays a positive role in HIV-1 virus production by binding to and thereby stabilizing HIV-1 RNA, together with ILF3.

References:

[1]. Yan Li, et al. NF45 and NF90 Bind HIV-1 RNA and Modulate HIV Gene Expression. Viruses. 2016 Feb 16;8(2):47. [Content Brief]

[2]. Sami Nourreddine, et al. NF45 and NF90 Regulate Mitotic Gene Expression by Competing with Staufen-Mediated mRNA Decay. Cell Rep. 2020 May 19;31(7):107660. [Content Brief]

[3]. Deyu Guan, et al. Nuclear factor 45 (NF45) is a regulatory subunit of complexes with NF90/110 involved in mitotic control. Mol Cell Biol. 2008 Jul;28(14):4629-41. [Content Brief]

[4]. Xiaofang Cui, et al. Cellular Interleukin Enhancer-Binding Factor 2, ILF2, Inhibits Japanese Encephalitis Virus Replication In Vitro. Viruses. 2019 Jun 17;11(6):559. [Content Brief]

[5]. N S Ting, et al. DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45. J Biol Chem. 1998 Jan 23;273(4):2136-45. [Content Brief]

[6]. M Satoh, et al. Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity. J Biol Chem. 1999 Dec 3;274(49):34598-604. [Content Brief]

[7]. Trevor W Reichman, et al. The RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cells. Mol Cell Biol. 2002 Jan;22(1):343-56. [Content Brief]

[8]. Ai Harashima, et al. Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defense. Genes Dev. 2010 Dec 1;24(23):2640-53. [Content Brief]

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