Proteomics

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The trypanosome Rhomboid protease RHBDL4 promotes retrotranslocation of aggregation-prone proteins for degradation

ABSTRACT: : In the endoplasmic reticulum (ER), the ER-associated degradation (ERAD) pathway targets incorrectly folded and unassembled proteins into the cytoplasm for turnover by the proteasome. Previously, we showed that the ER-resident rhomboid protease RHBDL4, together with p97, mediates membrane protein degradation. However, whether RHBDL4 acts in concert with additional ERAD components is unclear, and its full substrate spectrum remains to be defined. SILAC-based shotgun proteomics and immunoprecipitation experiments revealed that endogenously-tagged RHBDL4 interacts with the ERAD erlin complex. The interaction was validated with immunoprecipitation experiments of endogenous RHBDL4, Erlin1 and Erlin2 to show robust co-purification of the respective interaction partner.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Thomas Ruppert  

LAB HEAD: Thomas Ruppert

PROVIDER: PXD027346 | Pride | 2022-10-14

REPOSITORIES: Pride

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Rhomboid protease RHBDL4 promotes retrotranslocation of aggregation-prone proteins for degradation.

Bock Josephine J   Kühnle Nathalie N   Knopf Julia D JD   Landscheidt Nina N   Lee Jin-Gu JG   Ye Yihong Y   Lemberg Marius K MK  

Cell reports 20220801 6

Protein degradation is fundamentally important to ensure cell homeostasis. In the endoplasmic reticulum (ER), the ER-associated degradation (ERAD) pathway targets incorrectly folded and unassembled proteins for turnover by the cytoplasmic proteasome. Previously, we showed that the rhomboid protease RHBDL4, together with p97, mediates membrane protein degradation. However, whether RHBDL4 acts in concert with additional ERAD components is unclear, and its full substrate spectrum remains to be defi  ...[more]

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