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PIAS1 and TIF1γ collaborate to promote SnoN SUMOylation and suppression of epithelial–mesenchymal transition
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PIAS1 and TIF1γ collaborate to promote SnoN SUMOylation and suppression of epithelial–mesenchymal transition
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Journal Article
PIAS1 and TIF1γ collaborate to promote SnoN SUMOylation and suppression of epithelial–mesenchymal transition
2021
Overview
SUMO E3 ligases specify protein substrates for SUMOylation. The SUMO E3 ligases PIAS1 and TIF1γ target the transcriptional regulator SnoN for SUMOylation leading to suppression of epithelial–mesenchymal transition (EMT). Whether and how TIF1γ and PIAS1 might coordinate SnoN SUMOylation and regulation of EMT remained unknown. Here, we reveal that SnoN associates simultaneously with both TIF1γ and PIAS1, leading to a trimeric protein complex. Hence, PIAS1 and TIF1γ collaborate to promote the SUMOylation of SnoN. Importantly, loss of function studies of PIAS1 and TIF1γ suggest that these E3 ligases act in an interdependent manner to suppress EMT of breast cell-derived tissue organoids. Collectively, our findings unveil a novel mechanism by which SUMO E3 ligases coordinate substrate SUMOylation with biological implications.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 13/106
/ 13/109
/ 13/89
/ 13/95
/ 14/34
/ 14/5
/ 14/63
/ 38/77
/ 631/337
/ 82/29
/ 82/80
/ 96/21
/ 96/44
/ Animals
/ Biomedical and Life Sciences
/ Breast
/ Cell Culture Techniques, Three Dimensional
/ Epithelial-Mesenchymal Transition - genetics
/ Humans
/ Intracellular Signaling Peptides and Proteins - genetics
/ Intracellular Signaling Peptides and Proteins - metabolism
/ Mice
/ Protein Inhibitors of Activated STAT - genetics
/ Protein Inhibitors of Activated STAT - metabolism
/ Proto-Oncogene Proteins - genetics
/ Proto-Oncogene Proteins - metabolism
/ Small Ubiquitin-Related Modifier Proteins - genetics
/ Small Ubiquitin-Related Modifier Proteins - metabolism
/ Transcription Factors - genetics
