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. Author manuscript; available in PMC: 2016 Apr 7.
Published in final edited form as: Nat Rev Mol Cell Biol. 2015 Dec 9;17(2):83–96. doi: 10.1038/nrm.2015.4

Figure 2. Cellular localization of adenosine deaminases acting on RNA 1 (ADAR1) and ADAR2.

Figure 2

a | Exportin 1 (XPO1) binds to the nuclear export signal (NES) located within the Zα domain of ADAR1p150 and regulates its nuclear export together with RAN·GTP. Nuclear export of ADAR1p110 is mediated by XPO5–RAN·GTP and regulated by double-stranded RNA (dsRNA) binding to its dsRNA-binding domains (dsRBDs). The nuclear localization signal (NLS) located in dsRBD3 is responsible for localization of both ADAR1p150 and p110 in the nucleus and nucleolus. Nuclear import of ADAR1p110 is mediated by binding of transportin 1 (TRN1) to dsRBD3, which is inhibited by binding of dsRNA. b | The nuclear and nucleolar localization of ADAR2 is regulated by binding of karyopherin subunit α1 (KPNA1) and KPNA3 to an NLS located in the amino-terminal region. Phosphorylation of Thr32 by a currently unknown kinase enables interaction of ADAR2 with the prolyl-isomerase PIN1 in a dsRNA-binding-dependent manner, which isomerizes Pro33 and positively controls the nuclear localization and stability of ADAR2. The E3 ubiquitin ligase WWP2 promotes rapid degradation of ADAR2 in the cytoplasm, which is why ADAR2 is usually not detected in the cytoplasm. Ub, ubiquitin.