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Investigating the interactome of TurboID-tagged RABGAP1L in the presence or absence of IFNa2 by proximity labeling proteomics

ABSTRACT: RABGAP1L, a Tre2/Bub2/Cdc16 (TBC) domain-containing protein involved in the regulation of small membrane-bound GTPases, was identified in an RNAi screen to robustly potentiate the antiviral action of Interferon (IFN) against influenza A viruses (IAVs). Functional studies revealed that the catalytically active TBC domain of RABGAP1L promotes antiviral activity. By using proximity-labeling approaches, the aim was to investigate the protein’s interactome and thereby identify its possible role in existing signaling pathways.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: Sonja Fernbach

LAB HEAD: Benjamin Geoffrey Hale

PROVIDER: PXD029960 | Pride | 2022-04-07

REPOSITORIES: Pride

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Restriction factor screening identifies RABGAP1L-mediated disruption of endocytosis as a host antiviral defense.

Fernbach Sonja S Spieler Eva E EE Busnadiego Idoia I Karakus Umut U Lkharrazi Anouk A Stertz Silke S Hale Benjamin G BG

Cell reports 20220301 12

Host interferons (IFNs) powerfully restrict viruses through the action of several hundred IFN-stimulated gene (ISG) products, many of which remain uncharacterized. Here, using RNAi screening, we identify several ISG restriction factors with previously undescribed contributions to IFN-mediated defense. Notably, RABGAP1L, a Tre2/Bub2/Cdc16 (TBC)-domain-containing protein involved in regulation of small membrane-bound GTPases, robustly potentiates IFN action against influenza A viruses (IAVs). Func ...[more]

PMID: 35320721

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