Abstract
Nuclear glycogen accumulation has been reported in multiple cancers. Sun et al. show that glycogen is de novo synthesized in the nucleus, and nuclear glycogenolysis provides a carbon pool for histone acetylation. Non-small cell lung cancers suppress nuclear glycogenolysis by down-regulating a key E3 ubiquitin ligase to drive cancer progression.
Original language | English |
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Pages (from-to) | 903-916.e7 |
Journal | Cell Metabolism |
Volume | 30 |
Issue number | 5 |
DOIs | |
State | Published - Nov 5 2019 |
Bibliographical note
Publisher Copyright:© 2019 Elsevier Inc.
Keywords
- E3 ubiquitin ligase
- EPM2B
- Lafora disease
- NHLRC1
- glycogen
- glycogen phosphorylase
- histone acetylation
- malin
- non-small cell lung cancer
- nuclear metabolism
ASJC Scopus subject areas
- Physiology
- Molecular Biology
- Cell Biology