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• W2024013811 abstract "p27(kip1) has been implicated in cell cycle regulation, functioning as an inhibitor of cyclin-dependent kinase activity. In addition, p27 was also shown to affect cell migration, with accumulation of cytoplasmic p27 associated with tumor invasiveness. However, the mechanism underlying p27 regulation as a cytoplasmic protein is poorly understood. Here we show that glucose starvation induces proteasome-dependent degradation of cytoplasmic p27, accompanied by a decrease in cell motility. We also show that the glucose limitation-induced p27 degradation is regulated through an ubiquitin E3 ligase complex involving Siah1 and SIP/CacyBP. SIP (-/-) embryonic fibroblasts have increased levels of cytosolic p27 and exhibit increased cell motility compared to wild-type cells. These observations suggest that the Siah1/SIP E3 ligase complex regulates cell motility through degradation of p27." @default.
• W2024013811 created "2016-06-24" @default.
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• W2024013811 date "2011-08-01" @default.
• W2024013811 modified "2023-09-25" @default.
• W2024013811 title "Siah1/SIP regulates p27^kip1stability and cell migration under metabolic stress" @default.
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• W2024013811 doi "https://doi.org/10.4161/cc.10.15.16912" @default.
• W2024013811 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3180198" @default.
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