Biochemical and Biophysical Research Communications
Regular ArticleThe Interferon Inducible Autoantigen, IFI 16: Localization to the Nucleolus and Identification of a DNA-Binding Domain
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Herpes Simplex Viruses Type 1 and Type 2
2022, Encyclopedia of Infection and ImmunityThe Antiviral Apparatus: STING and Oncolytic Virus Restriction
2019, Molecular Therapy OncolyticsCitation Excerpt :For the canonical pathway, instead of placing IFI16 in the cytosolic role of STING activation, Diner suggested that IFI16 might operate in a purely nuclear role, as a downstream effector of IRF3. The seemingly variable behavior of IFI16 during DNA virus infection is consistent with its role as a functionally diverse gene product whose localization is cell-type specific and thus influenced by a range of conditions, including gene polymorphisms, post-translational modifications, hormonal regulation, and protein-protein interactions.35–40 Similarly, cGAS function and cellular localization may also vary.
IFI16, an amplifier of DNA-damage response: Role in cellular senescence and aging-associated inflammatory diseases
2016, Ageing Research ReviewsCitation Excerpt :However, the role of extracellular and “exosomal” IFI16 protein remains unknown. Earlier studies had predicted binding of IFI16 protein to DNA (Dawson and Trapani, 1995b). Accordingly, the IFI16 protein was identified as a cytosolic sensor for double-stranded DNA (DNA) (Unterholzner et al., 2010).
Mislocalization of the interferon inducible protein IFI16 by environmental insults: Implications in autoimmunity
2015, Cytokine and Growth Factor ReviewsCitation Excerpt :The IFI16 protein was discovered two decades ago as a protein constitutively expressed in the nucleus and nucleoli of lymphoid cells that can be induced by Interferons in myeloid cells [1–3].
Innate Recognition of Alphaherpesvirus DNA
2015, Advances in Virus ResearchIFI16: At the interphase between innate DNA sensing and genome regulation
2014, Cytokine and Growth Factor ReviewsCitation Excerpt :IFI16 was first described in lymphoid cells in 1992 and subsequently shown to be associated with myeloid cell differentiation [7,8]. Dawson and Trapani were the first to propose that IFI16 could bind nucleic acids [9] and they characterized a DNA binding domain within the C-terminal region of the IFI16 protein [10]. Today IFI16 is clustered into the PYHIN family of proteins defined by an N-terminal PYRIN domain (PYD), involved in homotypic protein–protein interactions, and one or two C-terminal DNA binding HIN domains (Fig. 2A).