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
Funding Information:This study was supported by National Institute of Health (NIH) grants R01 N070899 and P01 NS097197 to M.S.G. American Cancer Society grants in the form of an institutional research grant no. 16-182-28 to R.C.S. and a research scholar grant 133123-RSG-19-081-01-TBG to C.F.B.; NCI K22 CA201036 to C.F.B. NCI R01 CA237643 to C.F.B. American Association for Cancer Research Innovation and Discovery Grant to C.F.B. and AHA Great Rivers Affiliate Postdoctoral fellowship (12POST12030381) to V.V.D. This research was also supported by funding from the University of Kentucky Markey Cancer Center, NIH National Center for Advancing Translational Sciences UL1TR001998, the NIH-funded University of Kentucky Center for Cancer and Metabolism P20 GM121327, and the Biospecimen Procurement & Translational Pathology Shared Resource Facility of the University of Kentucky Markey Cancer Center P30CA177558.We would like to thank Dr. Otto Baba for providing the anti-glycogen antibody, Dr. Craig Vander Kooi and Gentry lab members for vigorous discussions regarding the work, Mrs. Dana Napier and Karrie Jones for performing immunohistochemistry on tissue slices, and the Markey Cancer Center, University of Kentucky for providing human NSCLC tissues that made this study possible. We also would like to thank Dr. Nancy Gough at Bioserendipity for editing this manuscript. Conceptualization, R.C.S. and M.S.G.; Methodology, R.C.S. M.S.G. and C.F.B.; Investigation, R.C.S. V.V.D. S.E. L.E.A.Y. Z.Q.Z. and C.F.B.; Writing – Original Draft, R.C.S. and M.S.G.; Writing – Review & Editing, R.C.S. and M.S.G.; Funding Acquisition, R.C.S. C.F.B. and M.S.G.; Resources, R.C.S. and M.S.G.; Supervision, R.C.S. C.F.B. and M.S.G. The authors declare no competing interests.
Funding Information:
This study was supported by National Institute of Health (NIH) grants R01 N070899 and P01 NS097197 to M.S.G., American Cancer Society grants in the form of an institutional research grant no. 16-182-28 to R.C.S., and a research scholar grant 133123-RSG-19-081-01-TBG to C.F.B.; NCI K22 CA201036 to C.F.B., NCI R01 CA237643 to C.F.B., American Association for Cancer Research Innovation and Discovery Grant to C.F.B., and AHA Great Rivers Affiliate Postdoctoral fellowship ( 12POST12030381 ) to V.V.D. This research was also supported by funding from the University of Kentucky Markey Cancer Center , NIH National Center for Advancing Translational Sciences UL1TR001998 , the NIH-funded University of Kentucky Center for Cancer and Metabolism P20 GM121327 , and the Biospecimen Procurement & Translational Pathology Shared Resource Facility of the University of Kentucky Markey Cancer Center P30CA177558 .We would like to thank Dr. Otto Baba for providing the anti-glycogen antibody, Dr. Craig Vander Kooi and Gentry lab members for vigorous discussions regarding the work, Mrs. Dana Napier and Karrie Jones for performing immunohistochemistry on tissue slices, and the Markey Cancer Center, University of Kentucky for providing human NSCLC tissues that made this study possible. We also would like to thank Dr. Nancy Gough at Bioserendipity for editing this manuscript.
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