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• W4296078746 endingPage "e202101359" @default.
• W4296078746 startingPage "e202101359" @default.
• W4296078746 abstract "The founding member of the F-box protein family, Cyclin-F, serves as a substrate adaptor for the E3 ligase Skp1-Cul1-F-box (SCF) Cyclin-F which is responsible for ubiquitination of proteins involved in cell cycle progression, DNA damage and mitotic fidelity. Missense mutations in CCNF encoding for Cyclin-F are associated with amyotrophic lateral sclerosis (ALS). However, it remains elusive whether CCNF mutations affect the substrate adaptor function of Cyclin-F and whether altered SCF Cyclin-F –mediated ubiquitination contributes to pathogenesis in CCNF mutation carriers. To address these questions, we set out to identify new SCF Cyclin-F targets in neuronal and ALS patient–derived cells. Mass spectrometry–based ubiquitinome profiling of CCNF knockout and mutant cell lines as well as Cyclin-F proximity and interaction proteomics converged on the HSP90 chaperone machinery as new substrate candidate. Biochemical analyses provided evidence for a Cyclin-F–dependent association and ubiquitination of HSP90AB1 and implied a regulatory role that could affect the binding of a number of HSP90 clients and co-factors. Together, our results point to a possible Cyclin-F loss-of-function–mediated chaperone dysregulation that might be relevant for ALS." @default.
• W4296078746 created "2022-09-17" @default.
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• W4296078746 date "2022-09-16" @default.
• W4296078746 modified "2023-10-05" @default.
• W4296078746 title "ALS-linked loss of Cyclin-F function affects HSP90" @default.
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• W4296078746 doi "https://doi.org/10.26508/lsa.202101359" @default.
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