Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Ring finger protein 213 assembles into a sensor for ISGylated proteins with antimicrobial activity.

Thery F, Martina L, Asselman C, Zhang Y, Vessely M, Repo H, Sedeyn K, Moschonas GD, Bredow C, Teo QW, Zhang J, Leandro K, Eggermont D, De Sutter D, Boucher K, Hochepied T, Festjens N, Callewaert N, Saelens X, Dermaut B, Knobeloch KP, Beling A, Sanyal S, Radoshevich L, Eyckerman S, Impens F

ISG15 is an interferon-stimulated, ubiquitin-like protein that can conjugate to substrate proteins (ISGylation) to counteract microbial infection, but the underlying mechanisms remain elusive. Here, we use a virus-like particle trapping technology to identify ISG15-binding proteins and discover Ring Finger Protein 213 (RNF213) as an ISG15 interactor and cellular sensor of ISGylated proteins. RNF213 is a poorly characterized, interferon-induced megaprotein that is ... [more]

Nat Commun Dec. 01, 2020; 12(1);5772 [Pubmed: 34599178]

Throughput

  • High Throughput

Additional Notes

  • #LPPI
  • Likely protein-protein interaction

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ISG15 DDOST
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Low-BioGRID
-

Curated By

  • BioGRID