Interferon-inducible double-stranded RNA-dependent protein kinase activator A

Definition:

Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner (By similarity).

References:

[1]. Yoontae Lee, et al. The role of PACT in the RNA silencing pathway. EMBO J. 2006 Feb 8;25(3):522-32. [Content Brief]

[2]. R C Patel, et al. PACT, a protein activator of the interferon-induced protein kinase, PKR. EMBO J. 1998 Aug 3;17(15):4379-90. [Content Brief]

[3]. G A Peters, et al. Modular structure of PACT: distinct domains for binding and activating PKR. Mol Cell Biol. 2001 Mar;21(6):1908-20. [Content Brief]

[4]. T Ito, et al. RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. J Biol Chem. 1999 May 28;274(22):15427-32. [Content Brief]

[5]. Kin Hang Kok, et al. Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA. J Biol Chem. 2007 Jun 15;282(24):17649-57. [Content Brief]

[6]. Gregory A Peters, et al. Phosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosis. J Biol Chem. 2006 Nov 17;281(46):35129-36. [Content Brief]

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