RNF26 binds perinuclear Vimentin filaments to integrate ER and endolysosomal responses to proteotoxic stress

ABSTRACT: Proteotoxic stress causes profound endoplasmic reticulum (ER) membrane remodeling into a perinuclear quality control compartment (ERQC) for the degradation of misfolded proteins. Subsequent return to homeostasis involves clearance of the ERQC by endolysosomes. However, the factors which control perinuclear ER integrity and dynamics remain unclear. Here, we identify vimentin intermediate filaments as perinuclear anchors for the ER and endolysosomes. We show that perinuclear vimentin filaments engage the ER-embedded RING finger protein 26 (RNF26) at the C-terminus of its RING domain. This restricts RNF26 to perinuclear ER subdomains and enables the corresponding spatial retention of endolysosomes through RNF26-mediated membrane contact sites (MCS). We find that both RNF26 and vimentin are re

SUBMITTER: Tom Cremer 

PROVIDER: S-SCDT-10_15252-EMBJ_2022111252 | biostudies-other |

REPOSITORIES: biostudies-other