JMJD6 regulates histone H2A.X phosphorylation and promotes autophagy in triple-negative breast cancer cells via a novel tyrosine kinase activity
Overexpression of Jumonji domain-containing 6 (JMJD6) has been reported to be associated with more aggressive breast cancer characteristics. However, the precise role of JMJD6 in breast cancer development remains unclear. Here, we demonstrate that JMJD6 has intrinsic tyrosine kinase activity and can...
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| Veröffentlicht in: | Oncogene 2019-02, Vol.38 (7), p.980-997 |
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| container_title | Oncogene |
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| creator | Liu, Yan Long, Yue-Hong Wang, Shu-Qing Zhang, Yuan-Yue Li, Yu-Feng Mi, Jiang-Sheng Yu, Cheng-Hua Li, De-Yan Zhang, Jing-Hua Zhang, Xiao-Jun |
| description | Overexpression of Jumonji domain-containing 6 (JMJD6) has been reported to be associated with more aggressive breast cancer characteristics. However, the precise role of JMJD6 in breast cancer development remains unclear. Here, we demonstrate that JMJD6 has intrinsic tyrosine kinase activity and can utilize ATP and GTP as phosphate donors to phosphorylate Y39 of histone H2A.X (H2A.X
Y39ph
). High JMJD6 levels promoted autophagy in triple negative breast cancer (TNBC) cells by regulating the expression of autophagy-related genes. The JMJD6-H2A.X
Y39ph
axis promoted TNBC cell growth via the autophagy pathway. We show that combined inhibition of JMJD6 kinase activity and autophagy efficiently decreases TNBC growth. Together, these findings suggest an effective strategy for TNBC treatment. |
| doi_str_mv | 10.1038/s41388-018-0466-y |
| format | Article |
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Y39ph
). High JMJD6 levels promoted autophagy in triple negative breast cancer (TNBC) cells by regulating the expression of autophagy-related genes. The JMJD6-H2A.X
Y39ph
axis promoted TNBC cell growth via the autophagy pathway. We show that combined inhibition of JMJD6 kinase activity and autophagy efficiently decreases TNBC growth. Together, these findings suggest an effective strategy for TNBC treatment.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/s41388-018-0466-y</identifier><identifier>PMID: 30185813</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13/1 ; 13/109 ; 13/44 ; 13/51 ; 14/19 ; 14/28 ; 38/39 ; 38/61 ; 38/77 ; 631/337/458/1733 ; 631/337/572 ; 631/67/1347 ; 631/67/395 ; 631/80/39 ; 64/60 ; 82/80 ; Amino acids ; Animals ; Apoptosis ; Autophagy ; Breast cancer ; Cancer cells ; Care and treatment ; Cell Biology ; Development and progression ; Female ; Gene expression ; Genetic aspects ; Guanosine triphosphate ; Health aspects ; Histone H2A ; Histones - genetics ; Histones - metabolism ; Human Genetics ; Humans ; Internal Medicine ; Jumonji Domain-Containing Histone Demethylases - genetics ; Jumonji Domain-Containing Histone Demethylases - metabolism ; Kinases ; Medicine ; Medicine & Public Health ; Mice ; Mice, Inbred BALB C ; Neoplasm Proteins - genetics ; Neoplasm Proteins - metabolism ; Oncology ; Oxidoreductases ; Phagocytosis ; Phenols (Class of compounds) ; Phosphates ; Phosphorylation ; Protein-tyrosine kinase ; Triple negative breast cancer ; Triple Negative Breast Neoplasms - genetics ; Triple Negative Breast Neoplasms - metabolism ; Triple Negative Breast Neoplasms - pathology ; Tyrosine</subject><ispartof>Oncogene, 2019-02, Vol.38 (7), p.980-997</ispartof><rights>Springer Nature Limited 2018</rights><rights>COPYRIGHT 2019 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Feb 2019</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-777c214e4f1a33057f3d91c90d0f6e5bfec044c646b517bdfdc1a4e3c0eb6f8f3</citedby><cites>FETCH-LOGICAL-c400t-777c214e4f1a33057f3d91c90d0f6e5bfec044c646b517bdfdc1a4e3c0eb6f8f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41388-018-0466-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41388-018-0466-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30185813$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Yan</creatorcontrib><creatorcontrib>Long, Yue-Hong</creatorcontrib><creatorcontrib>Wang, Shu-Qing</creatorcontrib><creatorcontrib>Zhang, Yuan-Yue</creatorcontrib><creatorcontrib>Li, Yu-Feng</creatorcontrib><creatorcontrib>Mi, Jiang-Sheng</creatorcontrib><creatorcontrib>Yu, Cheng-Hua</creatorcontrib><creatorcontrib>Li, De-Yan</creatorcontrib><creatorcontrib>Zhang, Jing-Hua</creatorcontrib><creatorcontrib>Zhang, Xiao-Jun</creatorcontrib><title>JMJD6 regulates histone H2A.X phosphorylation and promotes autophagy in triple-negative breast cancer cells via a novel tyrosine kinase activity</title><title>Oncogene</title><addtitle>Oncogene</addtitle><addtitle>Oncogene</addtitle><description>Overexpression of Jumonji domain-containing 6 (JMJD6) has been reported to be associated with more aggressive breast cancer characteristics. However, the precise role of JMJD6 in breast cancer development remains unclear. Here, we demonstrate that JMJD6 has intrinsic tyrosine kinase activity and can utilize ATP and GTP as phosphate donors to phosphorylate Y39 of histone H2A.X (H2A.X
Y39ph
). High JMJD6 levels promoted autophagy in triple negative breast cancer (TNBC) cells by regulating the expression of autophagy-related genes. The JMJD6-H2A.X
Y39ph
axis promoted TNBC cell growth via the autophagy pathway. We show that combined inhibition of JMJD6 kinase activity and autophagy efficiently decreases TNBC growth. Together, these findings suggest an effective strategy for TNBC treatment.</description><subject>13/1</subject><subject>13/109</subject><subject>13/44</subject><subject>13/51</subject><subject>14/19</subject><subject>14/28</subject><subject>38/39</subject><subject>38/61</subject><subject>38/77</subject><subject>631/337/458/1733</subject><subject>631/337/572</subject><subject>631/67/1347</subject><subject>631/67/395</subject><subject>631/80/39</subject><subject>64/60</subject><subject>82/80</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Autophagy</subject><subject>Breast cancer</subject><subject>Cancer cells</subject><subject>Care and treatment</subject><subject>Cell Biology</subject><subject>Development and progression</subject><subject>Female</subject><subject>Gene expression</subject><subject>Genetic aspects</subject><subject>Guanosine triphosphate</subject><subject>Health aspects</subject><subject>Histone H2A</subject><subject>Histones - genetics</subject><subject>Histones - metabolism</subject><subject>Human Genetics</subject><subject>Humans</subject><subject>Internal Medicine</subject><subject>Jumonji Domain-Containing Histone Demethylases - genetics</subject><subject>Jumonji Domain-Containing Histone Demethylases - metabolism</subject><subject>Kinases</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Oncology</subject><subject>Oxidoreductases</subject><subject>Phagocytosis</subject><subject>Phenols (Class of compounds)</subject><subject>Phosphates</subject><subject>Phosphorylation</subject><subject>Protein-tyrosine kinase</subject><subject>Triple negative breast cancer</subject><subject>Triple Negative Breast Neoplasms - genetics</subject><subject>Triple Negative Breast Neoplasms - metabolism</subject><subject>Triple Negative Breast Neoplasms - 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Academic</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Yan</au><au>Long, Yue-Hong</au><au>Wang, Shu-Qing</au><au>Zhang, Yuan-Yue</au><au>Li, Yu-Feng</au><au>Mi, Jiang-Sheng</au><au>Yu, Cheng-Hua</au><au>Li, De-Yan</au><au>Zhang, Jing-Hua</au><au>Zhang, Xiao-Jun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>JMJD6 regulates histone H2A.X phosphorylation and promotes autophagy in triple-negative breast cancer cells via a novel tyrosine kinase activity</atitle><jtitle>Oncogene</jtitle><stitle>Oncogene</stitle><addtitle>Oncogene</addtitle><date>2019-02</date><risdate>2019</risdate><volume>38</volume><issue>7</issue><spage>980</spage><epage>997</epage><pages>980-997</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><abstract>Overexpression of Jumonji domain-containing 6 (JMJD6) has been reported to be associated with more aggressive breast cancer characteristics. However, the precise role of JMJD6 in breast cancer development remains unclear. Here, we demonstrate that JMJD6 has intrinsic tyrosine kinase activity and can utilize ATP and GTP as phosphate donors to phosphorylate Y39 of histone H2A.X (H2A.X
Y39ph
). High JMJD6 levels promoted autophagy in triple negative breast cancer (TNBC) cells by regulating the expression of autophagy-related genes. The JMJD6-H2A.X
Y39ph
axis promoted TNBC cell growth via the autophagy pathway. We show that combined inhibition of JMJD6 kinase activity and autophagy efficiently decreases TNBC growth. Together, these findings suggest an effective strategy for TNBC treatment.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>30185813</pmid><doi>10.1038/s41388-018-0466-y</doi><tpages>18</tpages></addata></record> |
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| ispartof | Oncogene, 2019-02, Vol.38 (7), p.980-997 |
| issn | 0950-9232 1476-5594 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals |
| subjects | 13/1 13/109 13/44 13/51 14/19 14/28 38/39 38/61 38/77 631/337/458/1733 631/337/572 631/67/1347 631/67/395 631/80/39 64/60 82/80 Amino acids Animals Apoptosis Autophagy Breast cancer Cancer cells Care and treatment Cell Biology Development and progression Female Gene expression Genetic aspects Guanosine triphosphate Health aspects Histone H2A Histones - genetics Histones - metabolism Human Genetics Humans Internal Medicine Jumonji Domain-Containing Histone Demethylases - genetics Jumonji Domain-Containing Histone Demethylases - metabolism Kinases Medicine Medicine & Public Health Mice Mice, Inbred BALB C Neoplasm Proteins - genetics Neoplasm Proteins - metabolism Oncology Oxidoreductases Phagocytosis Phenols (Class of compounds) Phosphates Phosphorylation Protein-tyrosine kinase Triple negative breast cancer Triple Negative Breast Neoplasms - genetics Triple Negative Breast Neoplasms - metabolism Triple Negative Breast Neoplasms - pathology Tyrosine |
| title | JMJD6 regulates histone H2A.X phosphorylation and promotes autophagy in triple-negative breast cancer cells via a novel tyrosine kinase activity |
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