Gene interactions and pathways from curated databases and text-mining
EMBO J 2010, PMID: 20389281

The SNAG domain of Snail1 functions as a molecular hook for recruiting lysine-specific demethylase 1.

Lin, Yiwei; Wu, Yadi; Li, Junlin; Dong, Chenfang; Ye, Xiaofeng; Chi, Young-In; Evers, B Mark; Zhou, Binhua P

Epithelial-mesenchymal transition (EMT) is a transdifferentiation programme. The mechanism underlying the epigenetic regulation of EMT remains unclear. In this study, we identified that Snail1 interacted with histone lysine-specific demethylase 1 (LSD1). We demonstrated that the SNAG domain of Snail1 and the amine oxidase domain of LSD1 were required for their mutual interaction. Interestingly, the sequence of the SNAG domain is similar to that of the histone H3 tail, and the interaction of Snail1 with LSD1 can be blocked by LSD1 enzymatic inhibitors and a histone H3 peptide. We found that the formation of a Snail1-LSD1-CoREST ternary complex was critical for the stability and function of these proteins. The co-expression of these molecules was found in cancer cell lines and breast tumour specimens. Furthermore, we showed that the SNAG domain of Snail1 was critical for recruiting LSD1 to its target gene promoters and resulted in suppression of cell migration and invasion. Our study suggests that the SNAG domain of Snail1 resembles a histone H3-like structure and functions as a molecular hook for recruiting LSD1 to repress gene expression in metastasis.

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Text Mining Data

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Manually curated Databases

  • IRef Biogrid Interaction: SNAI1 — HIST1H3B, HIST1H3C, HIST1H3A, HIST1H3F, HIST1H3G, HIST1H3D, HIST1H3E, HIST1H3J, HIST1H3H, HIST1H3I (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: SNAI1 — HIST1H3B, HIST1H3C, HIST1H3A, HIST1H3F, HIST1H3G, HIST1H3D, HIST1H3E, HIST1H3J, HIST1H3H, HIST1H3I (direct interaction, enzymatic study)
  • IRef Biogrid Interaction: SNAI1 — KDM1A (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: SNAI1 — KDM1A (colocalization, imaging technique)
  • IRef Biogrid Interaction: RCOR1 — KDM1A (physical association, affinity chromatography technology)
  • IRef Intact Interaction: SNAI1 — HIST1H3B, HIST1H3C, HIST1H3A, HIST1H3F, HIST1H3G, HIST1H3D, HIST1H3E, HIST1H3J, HIST1H3H, HIST1H3I (physical association, competition binding)
  • IRef Intact Interaction: Complex of SNAI1-BTRC-KDM1A-GSK3B-PRMT5 (association, anti tag coimmunoprecipitation)
  • IRef Intact Interaction: SNAI1 — KDM1A (physical association, competition binding)
  • IRef Intact Interaction: SNAI1 — KDM1A (physical association, anti tag coimmunoprecipitation)
  • IRef Intact Interaction: SNAI1 — KDM1A (physical association, anti bait coimmunoprecipitation)
  • IRef Intact Interaction: SNAI1 — KDM1A (colocalization, fluorescence microscopy)
  • IRef Intact Interaction: SNAI1 — KDM1A (physical association, pull down)
In total, 21 gene pairs are associated to this article in curated databases