The Current Status of SSRP1 in Cancer: Tribulation and Road Ahead

Background and Objectives. Owing to the complexity and heterogeneity of tumors, cancer’s early diagnoses and treatment have become a provocation. Structure-specific recognition protein-1 (SSRP1) is a histone (H3-H4 or H2A-H2B) chaperone in chromatin-related processes such as transcription, cell cycle control, and DNA replication, reported in various tumor tissues. It may also be used as a biomarker. This study aimed to highlight the role of SSRP1 in cancer with a focus on the current progress and future perspective. Methods. We search PubMed and Web of Sciences with keywords “SSRP1” and “Cancer.” Only English literature was included, and conference papers and abstract were all excluded. Results. Transcription factors are classified into three groups based on their DNA binding motifs: simple helix-loop-helix (bHLH), classical zinc fingers (ZF-TFs), and homeodomains. The tumor-suppressive miR-497 (microRNA-497) acted as an undesirable regulator of SSRP1 upregulation, which led to tumor growth. The siRNA (small interfering RNA) knockdown of SSRP1 hindered cell proliferation along with incursion and glioma cell migration. Through the AKT (also known as protein kinase B) signaling pathway, SSRP1 silencing affected cancer apoptosis and cell proliferation. Conclusion. The MAPK (mitogen-activated protein kinase) signaling pathway’s phosphorylation was suppressed when SSRP1 was depleted. The effect of curaxins on p53 and NF-B (nuclear factor-κB), and their toxicity to cancer cells, is attributable to the FACT (facilitates chromatin transcription) complex’s chromatin trapping.