O-GlcNAcylation regulates breast cancer metastasis via SIRT1 modulation of FOXM1 pathway
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....
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| Veröffentlicht in: | Oncogene 2017-01, Vol.36 (4), p.559-569 |
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| creator | Ferrer, C M Lu, T Y Bacigalupa, Z A Katsetos, C D Sinclair, D A Reginato, M J |
| description | 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 (AMP-activated protein kinase α)-dependent manner. Reduced O-GlcNAcylation in cancer cells leads to SIRT1-mediated proteasomal degradation of oncogenic transcription factor FOXM1 in an 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 an SIRT1/ERK/FOXM1 axis. |
| doi_str_mv | 10.1038/onc.2016.228 |
| format | Article |
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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 (AMP-activated protein kinase α)-dependent manner. Reduced O-GlcNAcylation in cancer cells leads to SIRT1-mediated proteasomal degradation of oncogenic transcription factor FOXM1 in an 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 an SIRT1/ERK/FOXM1 axis.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/onc.2016.228</identifier><identifier>PMID: 27345396</identifier><identifier>CODEN: ONCNES</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/67/1347 ; 631/67/2327 ; 631/67/322 ; 96 ; 96/95 ; Animals ; Apoptosis ; Breast cancer ; Breast Neoplasms - genetics ; Breast Neoplasms - metabolism ; Breast Neoplasms - pathology ; Cancer metastasis ; Care and treatment ; Cell adhesion & migration ; Cell Biology ; Cell Line, Tumor ; Cell Proliferation - physiology ; Diagnosis ; Female ; Forkhead Box Protein M1 - genetics ; Forkhead Box Protein M1 - metabolism ; Glycosylation ; Health aspects ; Heterografts ; Human Genetics ; Humans ; Internal Medicine ; MCF-7 Cells ; Medicine ; Medicine & Public Health ; Metastasis ; Mice ; Mice, Inbred NOD ; N-Acetylglucosaminyltransferases - metabolism ; Neoplasm Metastasis ; Oncology ; original-article ; Physiological aspects ; Sirtuin 1 - genetics ; Sirtuin 1 - metabolism ; Tumors ; Ubiquitin</subject><ispartof>Oncogene, 2017-01, Vol.36 (4), p.559-569</ispartof><rights>Macmillan Publishers Limited 2017</rights><rights>COPYRIGHT 2017 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jan 26, 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c616t-8b01f77ff367dbfc737fc8a636a3d3a59eb02e1f03a249094903af2fdcb412943</citedby><cites>FETCH-LOGICAL-c616t-8b01f77ff367dbfc737fc8a636a3d3a59eb02e1f03a249094903af2fdcb412943</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,782,786,887,27933,27934</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27345396$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ferrer, C M</creatorcontrib><creatorcontrib>Lu, T Y</creatorcontrib><creatorcontrib>Bacigalupa, Z A</creatorcontrib><creatorcontrib>Katsetos, C D</creatorcontrib><creatorcontrib>Sinclair, D A</creatorcontrib><creatorcontrib>Reginato, M J</creatorcontrib><title>O-GlcNAcylation regulates breast cancer metastasis via SIRT1 modulation of FOXM1 pathway</title><title>Oncogene</title><addtitle>Oncogene</addtitle><addtitle>Oncogene</addtitle><description>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 (AMP-activated protein kinase α)-dependent manner. Reduced O-GlcNAcylation in cancer cells leads to SIRT1-mediated proteasomal degradation of oncogenic transcription factor FOXM1 in an 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 an SIRT1/ERK/FOXM1 axis.</description><subject>631/67/1347</subject><subject>631/67/2327</subject><subject>631/67/322</subject><subject>96</subject><subject>96/95</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Breast cancer</subject><subject>Breast Neoplasms - genetics</subject><subject>Breast Neoplasms - metabolism</subject><subject>Breast Neoplasms - pathology</subject><subject>Cancer metastasis</subject><subject>Care and treatment</subject><subject>Cell adhesion & migration</subject><subject>Cell Biology</subject><subject>Cell Line, Tumor</subject><subject>Cell Proliferation - physiology</subject><subject>Diagnosis</subject><subject>Female</subject><subject>Forkhead Box Protein M1 - genetics</subject><subject>Forkhead Box Protein M1 - metabolism</subject><subject>Glycosylation</subject><subject>Health aspects</subject><subject>Heterografts</subject><subject>Human Genetics</subject><subject>Humans</subject><subject>Internal Medicine</subject><subject>MCF-7 Cells</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Metastasis</subject><subject>Mice</subject><subject>Mice, Inbred NOD</subject><subject>N-Acetylglucosaminyltransferases - metabolism</subject><subject>Neoplasm Metastasis</subject><subject>Oncology</subject><subject>original-article</subject><subject>Physiological aspects</subject><subject>Sirtuin 1 - genetics</subject><subject>Sirtuin 1 - metabolism</subject><subject>Tumors</subject><subject>Ubiquitin</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNks9rFDEUx4Modq3ePMuAFw_Omh-TXxdhKbYWqgtaobeQySTblJlkTWYq-9-bYdfaSg8SQl7yPu_Ly-MLwGsElwgS8SEGs8QQsSXG4glYoIazmlLZPAULKCmsJSb4CLzI-QZCyCXEz8ER5qShRLIFuFrXZ735ujK7Xo8-hirZzVRCm6s2WZ3HyuhgbKoGO5abzj5Xt15X38-_XaJqiN10qIuuOl1ffUHVVo_Xv_TuJXjmdJ_tq8N5DH6cfro8-VxfrM_OT1YXtWGIjbVoIXKcO0cY71pnOOHOCM0I06QjmkrbQmyRg0TjRkJZNtEOu860DcKyIcfg4153O7WD7YwNY9K92iY_6LRTUXv1MBP8tdrEW0WRxBCyIvDuIJDiz8nmUQ0-G9v3Otg4ZYUEEwQ1lDf_gWLGoYCIFvTtP-hNnFIok5gFC4gpIX-pje6t8sHF0qKZRdWq4UJSQcjc4fIRqqzODt7EYJ0v7w8K3u8LTIo5J-vuxoGgmk2jimnUbBpVTFPwN_dHeAf_cUkB6j2QSypsbLr3mccEfwPcR8n3</recordid><startdate>20170126</startdate><enddate>20170126</enddate><creator>Ferrer, C M</creator><creator>Lu, T Y</creator><creator>Bacigalupa, Z A</creator><creator>Katsetos, C D</creator><creator>Sinclair, D A</creator><creator>Reginato, M J</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20170126</creationdate><title>O-GlcNAcylation regulates breast cancer metastasis via SIRT1 modulation of FOXM1 pathway</title><author>Ferrer, C M ; Lu, T Y ; Bacigalupa, Z A ; Katsetos, C D ; Sinclair, D A ; Reginato, M J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c616t-8b01f77ff367dbfc737fc8a636a3d3a59eb02e1f03a249094903af2fdcb412943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>631/67/1347</topic><topic>631/67/2327</topic><topic>631/67/322</topic><topic>96</topic><topic>96/95</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Breast cancer</topic><topic>Breast Neoplasms - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ferrer, C M</au><au>Lu, T Y</au><au>Bacigalupa, Z A</au><au>Katsetos, C D</au><au>Sinclair, D A</au><au>Reginato, M J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>O-GlcNAcylation regulates breast cancer metastasis via SIRT1 modulation of FOXM1 pathway</atitle><jtitle>Oncogene</jtitle><stitle>Oncogene</stitle><addtitle>Oncogene</addtitle><date>2017-01-26</date><risdate>2017</risdate><volume>36</volume><issue>4</issue><spage>559</spage><epage>569</epage><pages>559-569</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><coden>ONCNES</coden><abstract>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 (AMP-activated protein kinase α)-dependent manner. Reduced O-GlcNAcylation in cancer cells leads to SIRT1-mediated proteasomal degradation of oncogenic transcription factor FOXM1 in an 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 an SIRT1/ERK/FOXM1 axis.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>27345396</pmid><doi>10.1038/onc.2016.228</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Oncogene, 2017-01, Vol.36 (4), p.559-569 |
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| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5192006 |
| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | 631/67/1347 631/67/2327 631/67/322 96 96/95 Animals Apoptosis Breast cancer Breast Neoplasms - genetics Breast Neoplasms - metabolism Breast Neoplasms - pathology Cancer metastasis Care and treatment Cell adhesion & migration Cell Biology Cell Line, Tumor Cell Proliferation - physiology Diagnosis Female Forkhead Box Protein M1 - genetics Forkhead Box Protein M1 - metabolism Glycosylation Health aspects Heterografts Human Genetics Humans Internal Medicine MCF-7 Cells Medicine Medicine & Public Health Metastasis Mice Mice, Inbred NOD N-Acetylglucosaminyltransferases - metabolism Neoplasm Metastasis Oncology original-article Physiological aspects Sirtuin 1 - genetics Sirtuin 1 - metabolism Tumors Ubiquitin |
| title | O-GlcNAcylation regulates breast cancer metastasis via SIRT1 modulation of FOXM1 pathway |
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