The ER-embedded UBE2J1/RNF26 ubiquitylation complex exerts spatiotemporal control over the endolysosomal pathway
| Autor: | Jacques Neefjes, Ilana Berlin, Fredrik Trulsson, Tom Cremer, Alfred C.O. Vertegaal, Marlieke L.M. Jongsma |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
0301 basic medicine
Endosome EGFR Context (language use) Ubiquitin-conjugating enzyme General Biochemistry Genetics and Molecular Biology 03 medical and health sciences 0302 clinical medicine Spatio-Temporal Analysis Ubiquitin ubiquitin Humans biology Chemistry Endoplasmic reticulum Ubiquitination Compartmentalization (psychology) Transmembrane protein Ubiquitin ligase Cell biology UBE2J1 endoplasmic reticulum 030104 developmental biology RNF26 endosomes Ubiquitin-Conjugating Enzymes biology.protein 030217 neurology & neurosurgery |
| Zdroj: | Cell Rep Cell Reports, 34(3). CELL PRESS |
| ISSN: | 2211-1247 |
| DOI: | 10.1016/j.celrep.2020.108659 |
| Popis: | The endolysosomal system fulfills a wide variety of cellular functions, many of which are modulated through interactions with other organelles. In particular, the ER exerts spatiotemporal constraints on the organization and motility of endosomes and lysosomes. We have recently described the ER transmembrane E3 ubiquitin ligase RNF26 as a regulator of endolysosomal perinuclear positioning and transport dynamics. Here, we report that the ubiquitin conjugating enzyme UBE2J1, also anchored in the ER membrane, partners with RNF26 in this context, and that the cellular activity of the resulting E2/E3 pair is localized in a perinuclear ER subdomain and supported by transmembrane interactions. Through modification of SQSTM1/p62 on lysine 435, the ER-embedded UBE2J1/RNF26 ubiquitylation complex recruits endosomal adaptors to immobilize their cognate vesicles in the perinuclear region of the cell. The resulting spatiotemporal compartmentalization promotes the trafficking of activated EGFR to lysosomes and facilitates the termination of EGF-induced AKT signaling. |
| Databáze: | OpenAIRE |
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