Scaffold function of long non-coding RNA HOTAIR in protein ubiquitination

Je-Hyun Yoon (), Kotb Abdelmohsen, Jiyoung Kim, Xiaoling Yang, Jennifer L. Martindale, Kumiko Tominaga-Yamanaka, Elizabeth J. White, Arturo V. Orjalo, John L. Rinn, Stefan G. Kreft, Gerald M. Wilson and Myriam Gorospe
Additional contact information
Je-Hyun Yoon: Laboratory of Genetics, National Institute on Aging-Intramural Research Program, NIH
Kotb Abdelmohsen: Laboratory of Genetics, National Institute on Aging-Intramural Research Program, NIH
Jiyoung Kim: Laboratory of Genetics, National Institute on Aging-Intramural Research Program, NIH
Xiaoling Yang: Laboratory of Genetics, National Institute on Aging-Intramural Research Program, NIH
Jennifer L. Martindale: Laboratory of Genetics, National Institute on Aging-Intramural Research Program, NIH
Kumiko Tominaga-Yamanaka: Laboratory of Genetics, National Institute on Aging-Intramural Research Program, NIH
Elizabeth J. White: University of Maryland School of Medicine
Arturo V. Orjalo: Biosearch Technologies, Inc.
John L. Rinn: Harvard University
Stefan G. Kreft: University of Konstanz
Gerald M. Wilson: University of Maryland School of Medicine
Myriam Gorospe: Laboratory of Genetics, National Institute on Aging-Intramural Research Program, NIH

Nature Communications, 2013, vol. 4, issue 1, 1-14

Abstract: Abstract Although mammalian long non-coding (lnc)RNAs are best known for modulating transcription, their post-transcriptional influence on mRNA splicing, stability and translation is emerging. Here we report a post-translational function for the lncRNA HOTAIR as an inducer of ubiquitin-mediated proteolysis. HOTAIR associates with E3 ubiquitin ligases bearing RNA-binding domains, Dzip3 and Mex3b, as well as with their respective ubiquitination substrates, Ataxin-1 and Snurportin-1. In this manner, HOTAIR facilitates the ubiquitination of Ataxin-1 by Dzip3 and Snurportin-1 by Mex3b in cells and in vitro, and accelerates their degradation. HOTAIR levels are highly upregulated in senescent cells, causing rapid decay of targets Ataxin-1 and Snurportin-1, and preventing premature senescence. These results uncover a role for a lncRNA, HOTAIR, as a platform for protein ubiquitination.

Date: 2013
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms3939 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3939

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms3939

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().