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

Int J Mol Sci. 2021 Oct 3;22(19):10716. doi: 10.3390/ijms221910716.

Abstract

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™ 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.

Keywords: CASK; G-quadruplex; miR-1587; microRNA-protein interaction; regulation.

MeSH terms

  • Computational Biology / methods
  • G-Quadruplexes
  • Gene Expression Regulation
  • Guanylate Kinases / chemistry
  • Guanylate Kinases / genetics
  • Guanylate Kinases / metabolism*
  • Humans
  • MicroRNAs / chemistry
  • MicroRNAs / genetics*
  • MicroRNAs / metabolism*
  • Models, Biological
  • Models, Molecular
  • Nucleic Acid Conformation
  • Protein Binding
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / metabolism*
  • Reelin Protein
  • Structure-Activity Relationship

Substances

  • MIRN1587 microRNA, human
  • MicroRNAs
  • RNA-Binding Proteins
  • Reelin Protein
  • CASK kinases
  • Guanylate Kinases
  • RELN protein, human