Interactome analysis reveals that lncRNA HULC promotes aerobic glycolysis through LDHA and PKM2
Chunqing Wang,
Yongmei Li,
Shuai Yan,
Hao Wang,
Xianfeng Shao,
Mingming Xiao,
Baicai Yang,
Guoxuan Qin,
Ruirui Kong,
Ruibing Chen () and
Ning Zhang ()
Additional contact information
Chunqing Wang: Tianjin Medical University
Yongmei Li: Tianjin Medical University
Shuai Yan: Tianjin Medical University
Hao Wang: Tianjin Medical University
Xianfeng Shao: Tianjin Medical University
Mingming Xiao: Tianjin Medical University
Baicai Yang: Tianjin Medical University
Guoxuan Qin: Tianjin University
Ruirui Kong: Peking University Health Science Center
Ruibing Chen: Tianjin University
Ning Zhang: Tianjin Medical University
Nature Communications, 2020, vol. 11, issue 1, 1-15
Abstract:
Abstract Interacting with proteins is a crucial way for long noncoding RNAs (lncRNAs) to exert their biological responses. Here we report a high throughput strategy to characterize lncRNA interacting proteins in vivo by combining tobramycin affinity purification and mass spectrometric analysis (TOBAP-MS). Using this method, we identify 140 candidate binding proteins for lncRNA highly upregulated in liver cancer (HULC). Intriguingly, HULC directly binds to two glycolytic enzymes, lactate dehydrogenase A (LDHA) and pyruvate kinase M2 (PKM2). Mechanistic study suggests that HULC functions as an adaptor molecule that enhances the binding of LDHA and PKM2 to fibroblast growth factor receptor type 1 (FGFR1), leading to elevated phosphorylation of these two enzymes and consequently promoting glycolysis. This study provides a convenient method to study lncRNA interactome in vivo and reveals a unique mechanism by which HULC promotes Warburg effect by orchestrating the enzymatic activities of glycolytic enzymes.
Date: 2020
References: Add references at CitEc
Citations: View citations in EconPapers (3)
Downloads: (external link)
https://www.nature.com/articles/s41467-020-16966-3 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:11:y:2020:i:1:d:10.1038_s41467-020-16966-3
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-020-16966-3
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 ().