Exploration of the Hsa-miR-1587-Protein Interaction and the Inhibition to CASK

Hsa-miR-1587 has been found to be capable of forming G-quadruplex structures and is overexpressed in multiple cancer cell lines. Here, we explored the interactions between miR-1587 and proteins. HuProt (TM) human proteome microarray was utilized to screen the binding proteins, and it was discovered that CASK could bind to miR-1587 on the base of the G-quadruplex structure. Moreover, reelin and p21, which are downstream of CASK, were downregulated both transcriptionally and translationally by miR-1587, uncovered by q-RT-PCR and Western blot assays. Bioinformatic analysis was performed on STRING and Panther platforms, leading to the discovery that miR-1587 may be involved in intracellular metabolic and transcriptional physiological processes. This study explores the interaction of hsa-miR-1587 with proteins and provides a new strategy for the regulation of G-rich microRNA's function.

Automated summary

Hsa-miR-1587 is capable of forming G-quadruplex structures and is overexpressed in multiple cancer cell lines. Through interactions with proteins like CASK, it affects the expression levels of downstream proteins reelin and p21, potentially involved in intracellular metabolic and transcriptional physiological processes. This study provides a new strategy for regulating the function of G-rich microRNAs.