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™ human proteome microarray was utilized to screen the binding proteins, and it was discovered that...

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Main Authors: Lulu Zhang, Jiang Zhou, Ming Xu, Gu Yuan
Format: Article
Language:English
Published: MDPI AG 2021-10-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/22/19/10716
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author Lulu Zhang
Jiang Zhou
Ming Xu
Gu Yuan
author_facet Lulu Zhang
Jiang Zhou
Ming Xu
Gu Yuan
author_sort Lulu Zhang
collection DOAJ
description 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.
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spelling doaj.art-6f515cdf57014a7990aa5c824a0c8fb52023-11-22T16:14:16ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-10-0122191071610.3390/ijms221910716Exploration of the Hsa-miR-1587–Protein Interaction and the Inhibition to CASKLulu Zhang0Jiang Zhou1Ming Xu2Gu Yuan3Research Center of Basic Medicine, Jinan Central Hospital Affiliated to Shandong First Medical University, Jinan 250013, ChinaBeijing National Laboratory for Molecular Sciences, Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, ChinaKey Laboratory of Cardiovascular Molecular Biology and Regulatory Peptides of Ministry of Health, Key Laboratory of Molecular Cardiovascular Sciences of Ministry of Education, Department of Cardiology, Institute of Vascular Medicine, Peking University Third Hospital, Bejing 100191, ChinaBeijing National Laboratory for Molecular Sciences, Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, ChinaHsa-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.https://www.mdpi.com/1422-0067/22/19/10716miR-1587microRNA-protein interactionCASKG-quadruplexregulation
spellingShingle Lulu Zhang
Jiang Zhou
Ming Xu
Gu Yuan
Exploration of the Hsa-miR-1587–Protein Interaction and the Inhibition to CASK
International Journal of Molecular Sciences
miR-1587
microRNA-protein interaction
CASK
G-quadruplex
regulation
title Exploration of the Hsa-miR-1587–Protein Interaction and the Inhibition to CASK
title_full Exploration of the Hsa-miR-1587–Protein Interaction and the Inhibition to CASK
title_fullStr Exploration of the Hsa-miR-1587–Protein Interaction and the Inhibition to CASK
title_full_unstemmed Exploration of the Hsa-miR-1587–Protein Interaction and the Inhibition to CASK
title_short Exploration of the Hsa-miR-1587–Protein Interaction and the Inhibition to CASK
title_sort exploration of the hsa mir 1587 protein interaction and the inhibition to cask
topic miR-1587
microRNA-protein interaction
CASK
G-quadruplex
regulation
url https://www.mdpi.com/1422-0067/22/19/10716
work_keys_str_mv AT luluzhang explorationofthehsamir1587proteininteractionandtheinhibitiontocask
AT jiangzhou explorationofthehsamir1587proteininteractionandtheinhibitiontocask
AT mingxu explorationofthehsamir1587proteininteractionandtheinhibitiontocask
AT guyuan explorationofthehsamir1587proteininteractionandtheinhibitiontocask