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Article ; Online: Identification of circRNAs linked to Alzheimer's disease and related dementias.

Puri, Sambhavi / Hu, Junming / Sun, Zhuorui / Lin, Mintao / Stein, Thor D / Farrer, Lindsay A / Wolozin, Benjamin / Zhang, Xiaoling

Alzheimer's & dementia : the journal of the Alzheimer's Association

2023 Volume 19, Issue 8, Page(s) 3389–3405

Abstract: Introduction: Circular RNAs (circRNAs) exhibit selective expression in the brain and differential regulation in Alzheimer's disease (AD). To explore the role of circRNAs in AD, we investigated how circRNA expression varies between brain regions and with ...

Abstract	Introduction: Circular RNAs (circRNAs) exhibit selective expression in the brain and differential regulation in Alzheimer's disease (AD). To explore the role of circRNAs in AD, we investigated how circRNA expression varies between brain regions and with AD-related stress in human neuronal precursor cells (NPCs). Methods: Ribosomal RNA-depleted hippocampus RNA-sequencing data were generated. Differentially regulated circRNAs in AD and related dementias were detected using CIRCexplorer3 and limma. circRNA results were validated using quantitative real-time PCR of cDNA from the brain and NPCs. Results: We identified 48 circRNAs that were significantly associated with AD. We observed that circRNA expression differed by dementia subtype. Using NPCs, we demonstrated that exposure to oligomeric tau elicits downregulation of circRNA similar to that observed in the AD brain. Discussion: Our study shows that differential expression of circRNA can vary by dementia subtype and brain region. We also demonstrated that circRNAs can be regulated by AD-linked neuronal stress independently from their cognate linear messenger RNAs (mRNAs).
MeSH term(s)	Humans ; RNA, Circular/genetics ; RNA, Circular/metabolism ; Alzheimer Disease/genetics ; MicroRNAs/genetics ; RNA, Messenger/metabolism ; Down-Regulation
Chemical Substances	RNA, Circular ; MicroRNAs ; RNA, Messenger
Language	English
Publishing date	2023-02-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1002/alz.12960
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Abstract	Sequestosome1 (SQSTM1) is an autophagy receptor that mediates degradation of intracellular cargo, including protein aggregates, through multiple protein interactions. These interactions form the SQSTM1 protein network that are mediated by SQSTM1 functional interaction domains, which include LIR, PB1, UBA and KIR. Despite various attempts to unravel the complexity of the SQSTM1 protein network, our understanding of the relationship of various components in cellular physiology and disease states continues to evolve. To investigate the SQSTM1 protein interaction network, we performed proximity profile labeling by fusing TurboID with the human protein SQSTM1 (TurboID::SQSTM1). This chimeric protein displayed well-established SQSTM1 features including: production of SQSTM1 intracellular bodies, binding to known SQSTM1 interacting partners via defined functional SQSTM1 interacting domains and capture of novel SQSTM1 interactors. Strikingly, aggregated tau protein altered the protein interaction network of SQSTM1 to include many stress-associated proteins. Overall, our work reveals the dynamic landscape of the SQSTM1 protein network and offers a resource to study SQSTM1 function in cellular physiology and disease state.
Language	English
Publishing date	2023-12-13
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.12.12.571324
Database	MEDical Literature Analysis and Retrieval System OnLINE

Abstract

Sequestosome1 (SQSTM1) is an autophagy receptor that mediates degradation of intracellular cargo, including protein aggregates, through multiple protein interactions. These interactions form the SQSTM1 protein network that are mediated by SQSTM1 functional interaction domains, which include LIR, PB1, UBA and KIR. Despite various attempts to unravel the complexity of the SQSTM1 protein network, our understanding of the relationship of various components in cellular physiology and disease states continues to evolve. To investigate the SQSTM1 protein interaction network, we performed proximity profile labeling by fusing TurboID with the human protein SQSTM1 (TurboID::SQSTM1). This chimeric protein displayed well-established SQSTM1 features including: production of SQSTM1 intracellular bodies, binding to known SQSTM1 interacting partners via defined functional SQSTM1 interacting domains and capture of novel SQSTM1 interactors. Strikingly, aggregated tau protein altered the protein interaction network of SQSTM1 to include many stress-associated proteins. Overall, our work reveals the dynamic landscape of the SQSTM1 protein network and offers a resource to study SQSTM1 function in cellular physiology and disease state.

Language

English

Publishing date

2023-12-13

Publishing country

United States

Document type

Preprint

DOI

10.1101/2023.12.12.571324

Database

MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Identification of circRNAs linked to Alzheimer's disease and related dementias.

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