MORC family CW-type zinc finger protein 3

Definition:

Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response. Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function. Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity. Binds RNA in vitro. Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3. The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0.; (Microbial infection) May be required for influenza A transcription during viral infection.

References:

[1]. Yasuhiro Mimura, et al. Two-step colocalization of MORC3 with PML nuclear bodies. J Cell Sci. 2010 Jun 15;123(Pt 12):2014-24. [Content Brief]

[2]. Moritz M Gaidt, et al. Self-guarding of MORC3 enables virulence factor-triggered immunity. Nature. 2021 Dec;600(7887):138-142. [Content Brief]

[3]. Keiko Takahashi, et al. Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol Biol Cell. 2007 May;18(5):1701-9. [Content Brief]

[4]. Lorena S Ver, et al. The Cellular Factor NXP2/MORC3 Is a Positive Regulator of Influenza Virus Multiplication. J Virol. 2015 Oct;89(19):10023-30. [Content Brief]

[5]. Yanli Liu, et al. Family-wide Characterization of Histone Binding Abilities of Human CW Domain-containing Proteins. J Biol Chem. 2016 Apr 22;291(17):9000-13. [Content Brief]

[6]. Elizabeth Sloan, et al. MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes Simplex Virus 1 and Human Cytomegalovirus. J Virol. 2016 Sep 12;90(19):8621-33. [Content Brief]

[7]. Yukio Kimura, et al. The newly identified human nuclear protein NXP-2 possesses three distinct domains, the nuclear matrix-binding, RNA-binding, and coiled-coil domains. J Biol Chem. 2002 Jun 7;277(23):20611-7. [Content Brief]

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