Destabilisation of Argonaute 2 generates a truncated protein: halfAgo2

Bajan, S; Johnston, M; Hutvagner, G

Destabilisation of Argonaute 2 generates a truncated protein: halfAgo2

Bajan, S

Johnston, M Hutvagner, G

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Publisher:: Sciencematters
Publication Type:: Journal Article
Citation:: Matters, 2018
Issue Date:: 2018-11-13

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Field	Value	Language
dc.contributor.author	Bajan, S https://orcid.org/0000-0001-6934-5240	en_US
dc.contributor.author	Johnston, M	en_US
dc.contributor.author	Hutvagner, G https://orcid.org/0000-0002-7231-9446	en_US
dc.date.issued	2018-11-13	en_US
dc.identifier.citation	Matters, 2018	en_US
dc.identifier.issn	2297-8240	en_US
dc.identifier.uri	http://hdl.handle.net/10453/129625
dc.description.abstract	The Argonaute 2 (Ago2) protein is an essential effector protein in miRNA-mediated mechanisms that regulate gene expression. Ago2 directly binds to the miRNA, forming the RISC. RISC function is critical to controlling key biological processes and when dysregulated can result in disease pathogenesis. Understanding Ago2 protein stability and turnover will further our understanding in how RISC function is regulated. In human cells, we discovered a previously unidentified ~55 kDa protein that is a truncated form of Ago2, that is formed from proteolytic cleavage of the full length Ago2 protein. Further experiments are needed to determine (i) the detailed mechanism that forms halfAgo2 (ii) the cellular or environmental triggers or stresses that initiate halfAgo2 production and (iii) if halfAgo2 has a potentially new role in gene regulation.	en_US
dc.language	en	en_US
dc.publisher	Sciencematters	en_US
dc.relation.ispartof	Matters	en_US
dc.relation.isbasedon	10.19185/matters.201811000001	en_US
dc.title	Destabilisation of Argonaute 2 generates a truncated protein: halfAgo2	en_US
dc.type	Journal Article
utslib.for	0903 Biomedical Engineering	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology/School of Biomedical Engineering
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
utslib.copyright.status	open_access
pubs.consider-herdc	true	en_US
pubs.publication-status	Published online	en_US

Abstract:

The Argonaute 2 (Ago2) protein is an essential effector protein in miRNA-mediated mechanisms that regulate gene expression. Ago2 directly binds to the miRNA, forming the RISC. RISC function is critical to controlling key biological processes and when dysregulated can result in disease pathogenesis. Understanding Ago2 protein stability and turnover will further our understanding in how RISC function is regulated. In human cells, we discovered a previously unidentified ~55 kDa protein that is a truncated form of Ago2, that is formed from proteolytic cleavage of the full length Ago2 protein. Further experiments are needed to determine (i) the detailed mechanism that forms halfAgo2 (ii) the cellular or environmental triggers or stresses that initiate halfAgo2 production and (iii) if halfAgo2 has a potentially new role in gene regulation.

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http://hdl.handle.net/10453/129625