Snail Family Zinc Finger 1, commonly referred to as SNAI1 or Snail, is a zinc finger transcriptional repressor protein encoded by the SNAI1 gene in humans . This protein plays a crucial role in the regulation of epithelial to mesenchymal transition (EMT) during embryonic development . EMT is a biological process where epithelial cells lose their cell polarity and cell-cell adhesion properties, gaining migratory and invasive characteristics to become mesenchymal stem cells .
SNAI1 is structurally similar to the Drosophila Snail protein and is critical for mesoderm formation in the developing embryo . The protein contains zinc finger domains that allow it to bind to specific DNA sequences, particularly E-boxes in the promoter regions of target genes . By binding to these regions, SNAI1 represses the expression of genes such as E-cadherin (CDH1), which is essential for maintaining epithelial cell adhesion . This repression facilitates the transition of tightly bound epithelial cells into migratory mesenchymal cells .
During embryonic development, SNAI1 is vital for the formation and maintenance of the mesoderm, a middle layer of cells that gives rise to various tissues and organs . The protein’s ability to induce EMT is also implicated in various pathological conditions, including cancer metastasis . In cancer, the reactivation of EMT programs, often driven by SNAI1, enables tumor cells to invade surrounding tissues and disseminate to distant sites .
SNAI1 is regulated by several signaling pathways, including the Wnt and prostaglandin pathways . Wnt3a, for instance, is a master regulator of paraxial presomatic mesoderm cells, which differentiate into the musculoskeletal system . Other genes, such as Msx1, Pax3, and Mesogenin 1 (Msgn1), also play roles in regulating SNAI1 to ensure proper EMT activation . Msgn1 activates SNAI1 by binding to its enhancer, creating a feed-forward mechanism that ensures redundancy in the system .