Nuclear Glycogenolysis Modulates Histone Acetylation in Human Non-Small Cell Lung Cancers

Ramon C. Sun, Vikas V. Dukhande, Zhengqiu Zhou, Lyndsay E.A. Young, Shane Emanuelle, Christine Fillmore Brainson, Matthew S. Gentry

Research output: Contribution to journalArticlepeer-review

70 Scopus citations

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 languageEnglish
Pages (from-to)903-916.e7
JournalCell Metabolism
Volume30
Issue number5
DOIs
StatePublished - 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

Fingerprint

Dive into the research topics of 'Nuclear Glycogenolysis Modulates Histone Acetylation in Human Non-Small Cell Lung Cancers'. Together they form a unique fingerprint.

Cite this