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O-GlcNAcylation regulates breast cancer metastasis via SIRT1 modulation of FOXM1 pathway
Journal article   Open access   Peer reviewed

O-GlcNAcylation regulates breast cancer metastasis via SIRT1 modulation of FOXM1 pathway

Christina M Ferrer, Tong Y Lu, Zachary A Bacigalupa, Christos D Katsetos, David A Sinclair and Mauricio J Reginato
Oncogene, v 36(4), pp 559-569
26 Jan 2017
PMID: 27345396
url
https://doi.org/10.1038/onc.2016.228View
Published, Version of Record (VoR) Open

Abstract

FOXM1 O-GlcNAc SIRT1 MEK sirtuin invasion metastasis deacetylation AMPK cancer metabolism OGT ERK
Tumors utilize aerobic glycolysis to support growth and invasion. However, the molecular mechanisms that link metabolism with invasion are not well understood. The nutrient sensor O-linked-β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) modifies intracellular proteins with N-acetylglucosamine. Cancers display elevated O-GlcNAcylation and suppression of O-GlcNAcylation inhibits cancer invasion and metastasis. Here, we show that the regulation of cancer invasion by OGT is dependent on the NAD + -dependent deacetylase SIRT1. Reducing O-GlcNAcylation elevates SIRT1 levels and activity in an AMPK-dependent manner. Reduced O-GlcNAcylation in cancer cells leads to SIRT1-mediated proteasomal degradation of oncogenic transcription factor FOXM1 in a MEK/ERK-dependent manner. SIRT1 is critical for OGT-mediated regulation of FOXM1 ubiquitination and reducing SIRT1 activity reverses OGT-mediated regulation of FOXM1. Moreover, we show that SIRT1 levels are required for OGT-mediated regulation of invasion and metastasis in breast cancer cells. Thus, O-GlcNAcylation is a central component linking metabolism to invasion and metastasis via a SIRT1/ /FOXM1 axis.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
Genetics & Heredity
Oncology
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