Jul 2, 2020 · RNF185 interactions were validated by co-expression and pulldown with S-tagged HCIPs (Figure 3—figure supplement 1C). Interestingly, the Ca 2+-load-activated Ca 2+ channel TMCO1, which prevents overfilling in the ER (Wang et al., 2016), was also enriched by RNF170.

Jul 2, 2020 · Transient expression of S-tagged HCIPs in Flp-In293 cells stably expressing FH-RNF185. Complexes were affinity purified from 1% LMNG-solubilised lysates by S-protein agarose, separated by SDS-PAGE and the resulting western blots probed for RNF185 (anti-HA) and the HCIP (anti-S-tag).

Sep 3, 2020 · Using biochemical and mass spectrometry approaches, we showed that this ERAD branch is defined by an ER membrane complex consisting of the ubiquitin ligase RNF185, the ubiquitin-like domain containing proteins TMUB1/2 and TMEM259/Membralin, a poorly characterized protein.

Oct 25, 2013 · RNF185 is a RING domain-containing polypeptide homologous to RNF5. We show that RNF185 controls the stability of CFTR and of the CFTRΔF508 mutant in a RING- and proteasome-dependent manner but does not control that of …

RNF185 is a RING domain-containing polypeptide homologous to RNF5. We show that RNF185 controls the stability of CFTR and of the CFTRΔF508 mutant in a RING- and proteasome-dependent manner but does not control that of other classical ERAD model substrates. Reciprocally, its silencing stabilizes CFTR proteins.

Sep 3, 2020 · Here, we analyzed the degradation pathways of two short-lived ER membrane model proteins in mammalian cells. Using a CRISPR-Cas9 genome-wide library screen, we identified an ERAD branch required for quality control of a subset of membrane proteins.

Results: RNF185 targets CFTR and CFTRF508 to co-translational degradation and synergizes with RNF5 to their post- translational degradation. Conclusion: RNF185 and RNF5 act together as major ERAD E3 ligases of CFTR.

Sep 9, 2011 · The polyubiquitinated BNIP1 is capable of recruiting autophagy receptor p62, which simultaneously binds both ubiquitin and LC3 to link ubiquitination and autophagy. Our study might reveal a novel RNF185-mediated mechanism for …

May 19, 2023 · Using genetic screens to dissect the molecular machinery involved in the degradation of candidate viral proteins, we identified human E3 ligase RNF185 as a regulator of protein stability for the SARS-CoV-2 envelope protein.

Our study uncovers RNF185 as the first E3 ubiquitin ligase of cGAS and suggests RNF185 as an important target for modulating antiviral response. The innate immune system serves as the first line of host defense against invading microbes.