Abstract
SNAIL (SNAI1) is a zinc finger transcription factor that binds to E-box sequences and regulates the expression of genes. It usually acts as a gene repressor, but it may also activate the expression of genes. SNAIL plays a key role in the regulation of epithelial to mesenchymal transition, which is the main mechanism responsible for the progression and metastasis of epithelial tumors. Nevertheless, it also regulates different processes that are responsible for tumor growth, such as the activity of cancer stem cells, the control of cell metabolism, and the regulation of differentiation. Different proteins and microRNAs may regulate the SNAIL level, and SNAIL may be an important regulator of microRNA expression as well. The interplay among SNAIL, microRNAs, long non-coding RNAs, and circular RNAs is a key event in the regulation of tumor growth and metastasis. This review for the first time discusses different types of regulation between SNAIL and non-coding RNAs with a focus on feedback loops and the role of competitive RNA. Understanding these mechanisms may help develop novel therapeutic strategies against cancer based on microRNAs.
Highlights
Background of SNAIL Transcription FactorSNAIL is a member of the group of conservative zinc finger transcription factors
SNAIL is a transcriptional repressor, which binds to regulatory regions and promoters containing sequences called E-boxes, and thereby it regulates the expression of many different genes and in this way, it may regulate epithelial to mesenchymal transition (EMT)
We present bidirectional crosstalk between SNAIL and non-coding RNAs with implications of these new findings on tumor progression, which may help develop novel therapeutic strategies in future
Summary
SNAIL is a member of the group of conservative zinc finger transcription factors. It was first described in Drosophila melanogaster as an essential factor for the mesoderm formation [1]. Its homologues have been described in many species, including humans. The SNAIL family consists of three members: SNAIL (SNAI1), SLUG (SNAI2), and SMUG (SNAI3) [2]. The SNAIL protein contains C-terminal zinc finger domains that are responsible for DNA binding, the N-terminal SNAG domain responsible for interaction with several co-repressors or epigenetic remodeling complexes, the serine-rich domain (SRD) regulating ubiquitination and proteasome degradation, and the nuclear export sequence (NES) that controls the protein stability and subcellular localization [3]
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