Insights Into SND1 Oncogene Promoter Regulation

Abstract

The staphylococcal nuclease and Tudor domain containing 1 gene (SND1), also known as Tudor-SN, TSN or p100, encodes an evolutionarily conserved protein with invariant domain composition. SND1 contains four repeated staphylococcal nuclease domains and a single Tudor domain, which confer it endonuclease activity and extraordinary capacity for interacting with nucleic acids, individual proteins and protein complexes. Originally described as a transcriptional coactivator, SND1 plays fundamental roles in the regulation of gene expression, including RNA splicing, interference, stability, and editing, as well as in the regulation of protein and lipid homeostasis. Recently, SND1 has gained attention as a potential disease biomarker due to its positive correlation with cancer progression and metastatic spread. Such functional diversity of SND1 marks this gene as interesting for further analysis in relation with the multiple levels of regulation of SND1 protein production. In this review, we summarize the SND1 genomic region and promoter architecture, the set of transcription factors that can bind the proximal promoter, and the evidence supporting transactivation of SND1 promoter by a number of signal transduction pathways operating in different cell types and conditions. Unraveling the mechanisms responsible for SND1 promoter regulation is of utmost interest to decipher the SND1 contribution in the realm of both normal and abnormal physiology.

The Tudor Domain-Containing Protein BbTdp1 Contributes to Fungal Cell Development, the Cell Cycle, Virulence, and Transcriptional Regulation in the Insect Pathogenic Fungus Beauveria bassiana

“…When blastospores were cultured under simulated conditions, the yield of blastospores was dramatically reduced in the Δ BbTdp1 mutant, indicating that BbTdp1 contributes to blastospore proliferation. In previous studies of oncogenes, SND1 was found to be highly expressed during the stage of malignant proliferation and aggressiveness of many common human cancer cells ( 10 ). In colon cancer, SND1 overexpression significantly accelerated cell proliferation in the exponential growth phase ( 31 ).…”

“…Similar to other SND1 orthologs (e.g., TSN, Tudor-SN, and p100), BbTdp1 contains four SNc domains and one tudor domain. As a transcription coactivator, SND1 is considered to be involved not only in the regulation of gene expression, such as RNA splicing, interference, stability, and editing, but also in the control of protein and lipid homeostasis ( 10 ). In human cells, mature functional microRNAs (miRNAs) are degraded by SND1, which promotes the progression of the cell cycle, indicating that targeting SND1 nuclease activity could inhibit cell proliferation ( 13 ).…”

“…Tudor domain-containing protein (Tdp1; a homologous protein of SND1) has been proven to be an evolutionarily conserved regulator composed of four staphylococcal nuclease (SNc) domains, providing endonuclease activity for SND1 and a tudor domain with the extraordinary ability to interact with nucleic acids and proteins ( 10 ). Originally, SND1 as a transcriptional coactivator was relevant for the regulation of gene expression-related processes as well as for the mediation of the dynamic balance of proteins and lipids ( 10 , 11 ). SND1 has also been shown to participate in cell cycle regulation by mediating the G 1 /S phase transition ( 12 , 13 ).…”

The interactome of the prostate-specific protein Anoctamin 7

“…According to the work of Dubois et al, HSPA1A is present in the lipid rafts of prostasomes [24]. SND1 was first identified as a transcription coactivator [39] but has also been shown to have several functions related to RNA metabolism [40]. The expression of SND1 is increased in many cancers, including PrCa.…”

The Role of the PRMT5–SND1 Axis in Hepatocellular Carcinoma

“…Furthermore, TGFβ signaling also induces SND1 transcriptional activation in a feed forward loop [ 140 ]. This feed forward activity can be seen in other SND1-regulated pathways including NF-κB and SREBPs [ 141 ]. SND1 further promotes proliferative signals by degradation of miRNA via its nuclease domains.…”