Expression of Snail1 correlates with the level of LSD1 and CoREST in tumour tissues. Expression of Snail1 correlates with the level of LSD1 and CoREST in tumour tissues. (A) The 116 surgical specimens of breast cancer were immunostained using antibodies against Snail1, LSD1, CoREST, and the control serum (data not shown). Representative stainings from the same tumour samples are shown. Scale bar=100 μm. (B) The expression patterns of Snail1, LSD1 and CoREST in the 116 breast tumour samples were determined and summarized. Correlation of Snail1 with LSD1 and CoREST was analysed using Fisher's exact test (P<0.001). P<0.05 was set as the criterion for statistical significance. (C) A proposed model to illustrate how Snail1 recruits the LSD1–CoREST complex to the E‐cadherin promoter. The SNAG domain of Snail1 assembles a histone H3‐like structure and serves as a molecular ‘hook’ (or pseudo‐substrate, a red dot indicates the critical residues in Snail1 and histone H3 that interact with LSD1) to interact with the LSD1–CoREST complex. The formation of this complex stabilizes the individual components from potential proteasomal degradation. Snail1 brings this complex to its targeted gene promoters through the binding of the E‐box through the zinc‐finger motifs. An overabundant amount of histone H3 at the chromatin region outcompetes the binding of the SNAG domain with the catalytic core of LSD1 and results in the demethylation of histone H3K4. Yiwei Lin et al. EMBO J. 2010;29:1803-1816 © as stated in the article, figure or figure legend