Exploration of the Hsa-miR-1587-Protein Interaction and the Inhibition to CASK.
Int J Mol Sci
; 22(19)2021 Oct 03.
Article
in En
| MEDLINE
| ID: mdl-34639058
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
RNA-Binding Proteins
/
MicroRNAs
/
Guanylate Kinases
Limits:
Humans
Language:
En
Journal:
Int J Mol Sci
Year:
2021
Document type:
Article
Affiliation country:
China