Identification of ADAR2-associated complexes

ABSTRACT: Adenosine deaminase acting on RNA 2 (ADAR2) catalyzes adenosine-to-inosine RNA editing and contributes to multiple aspects of post-transcriptional regulation. Proximity-labeling (BioID) studies have previously defined the proximal protein environment of ADAR2. To complement these datasets and identify stably associated proteins, we performed Strep-tag affinity purification coupled to label-free LC–MS/MS. Doxycycline-inducible 293 T-REx cells expressing N-terminally Strep II–HA–tagged ADAR2 were used to isolate ADAR2-containing complexes under native conditions, followed by high-resolution mass spectrometric identification and quantification of co-purifying proteins. The resulting ADAR2 interactome shows significant overlap with our previously defined ADAR1 interaction network, as well as with publicly available ADAR2 proximity-labeling datasets, supporting the robustness and reproducibility of ADAR-associated protein complexes across methods and studies. This dataset provides a focused map of the stable ADAR2 interactome. This proteomic data form the basis of the first figure in the associated ADAR–exosome manuscript and complement existing proximity-labeling data by defining stable ADAR2 protein complexes.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Dragana Vukic  

LAB HEAD: Prof. Mary Anne O´Connell, Ph.D.

PROVIDER: PXD071677 | Pride | 2026-04-30

REPOSITORIES: Pride