Demonstrates that ADAR1 and ADAR2 form homo- and heterodimers in vivo in an RNA-independent manner, which may be important for their RNA-editing activity.
Answers are grounded in this paper and cite their sources.
Dimerization may regulate ADAR editing; hypothesis-generating for cardiovascular RNA dysregulation and requires validation before clinical consideration.
Members of the ADAR (adenosine deaminase that acts on RNA) enzyme family catalyze the hydrolytic deamination of adenosine to inosine within double-stranded RNAs, a poorly understood process that is critical to mammalian development. We have performed fluorescence resonance energy transfer experiments in mammalian cells transfected with fluorophore-bearing ADAR1 and ADAR2 fusion proteins to investigate the relationship between these proteins. These studies conclusively demonstrate the homodimerization of ADAR1 and ADAR2 and also show that ADAR1 and ADAR2 form heterodimers in human cells. RNase treatment of cells expressing these fusion proteins changes their localization but does not affect dimerization. Taken together these results suggest that homo- and heterodimerization are important for the activity of ADAR family members in vivo and that these associations are RNA independent.
No takes yet. Share an insight, caveat, or question.
Chilibeck et al. (2006) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: