Regulation of Ultraviolet B-induced Phosphorylation of Histone H3 at Serine 10 by Fyn Kinase
Ultraviolet B (UVB) induces phosphorylation of histone H3 at serine 10, and mitogen-activated protein kinases are involved in this signal transduction pathway. Here we provide evidence that Fyn kinase, a member of the Src kinase family, is involved in the UVB-induced phosphorylation of histone H3 at...
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| Veröffentlicht in: | The Journal of biological chemistry 2005-01, Vol.280 (4), p.2446-2454 |
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| creator | He, Zhiwei Cho, Yong-Yeon Ma, Wei-Ya Choi, Hong Seok Bode, Ann M. Dong, Zigang |
| description | Ultraviolet B (UVB) induces phosphorylation of histone H3 at serine 10, and mitogen-activated protein kinases are involved in this signal transduction pathway. Here we provide evidence that Fyn kinase, a member of the Src kinase family, is involved in the UVB-induced phosphorylation of histone H3 at serine 10. UVB distinctly increased Fyn kinase activity and phosphorylation. Fyn kinase inhibitors 4-amino-5-(4-chlorophenyl)-7(t-butyl)pyrazol(3,4-d)pyramide and leflunomide, an Src kinase inhibitor, suppressed both UVB-induced phosphorylation of histone H3 at serine 10 and Fyn kinase activity and phosphorylation. UVB-induced phosphorylation of histone H3 at serine 10 was blocked by either a dominant-negative mutant of Fyn (DNM-Fyn) kinase or small interfering RNA of Fyn kinase. UVB-induced phosphorylation and activities of ERKs and protein kinase B/Akt were markedly inhibited by DNM-Fyn kinase. However, DNM-Fyn kinase did not inhibit UVB-induced phosphorylation of p38 MAPK or c-Jun N-terminal kinases. Active Fyn kinase phosphorylated histone H3 at serine 10 in vitro, and the phosphorylated Fyn kinase could translocate into the nucleus of HaCaT cells. These results indicate that Fyn kinase plays a key role in the UVB-induced phosphorylation of histone H3 at serine 10. |
| doi_str_mv | 10.1074/jbc.M402053200 |
| format | Article |
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Here we provide evidence that Fyn kinase, a member of the Src kinase family, is involved in the UVB-induced phosphorylation of histone H3 at serine 10. UVB distinctly increased Fyn kinase activity and phosphorylation. Fyn kinase inhibitors 4-amino-5-(4-chlorophenyl)-7(t-butyl)pyrazol(3,4-d)pyramide and leflunomide, an Src kinase inhibitor, suppressed both UVB-induced phosphorylation of histone H3 at serine 10 and Fyn kinase activity and phosphorylation. UVB-induced phosphorylation of histone H3 at serine 10 was blocked by either a dominant-negative mutant of Fyn (DNM-Fyn) kinase or small interfering RNA of Fyn kinase. UVB-induced phosphorylation and activities of ERKs and protein kinase B/Akt were markedly inhibited by DNM-Fyn kinase. However, DNM-Fyn kinase did not inhibit UVB-induced phosphorylation of p38 MAPK or c-Jun N-terminal kinases. Active Fyn kinase phosphorylated histone H3 at serine 10 in vitro, and the phosphorylated Fyn kinase could translocate into the nucleus of HaCaT cells. These results indicate that Fyn kinase plays a key role in the UVB-induced phosphorylation of histone H3 at serine 10.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M402053200</identifier><identifier>PMID: 15537652</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cell Line ; Cell Line, Tumor ; Dose-Response Relationship, Drug ; Genes, Dominant ; Histones - chemistry ; Histones - metabolism ; Humans ; Isoxazoles - pharmacology ; Leflunomide ; MAP Kinase Signaling System ; Mice ; Models, Biological ; p38 Mitogen-Activated Protein Kinases - metabolism ; Phosphorylation ; Plasmids - metabolism ; Protein-Serine-Threonine Kinases - metabolism ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-akt ; Proto-Oncogene Proteins c-fyn ; RNA, Small Interfering - metabolism ; Serine - chemistry ; Serine - metabolism ; Signal Transduction ; src-Family Kinases - metabolism ; Threonine - chemistry ; Time Factors ; Transfection ; Ultraviolet Rays</subject><ispartof>The Journal of biological chemistry, 2005-01, Vol.280 (4), p.2446-2454</ispartof><rights>2005 © 2005 ASBMB. 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Here we provide evidence that Fyn kinase, a member of the Src kinase family, is involved in the UVB-induced phosphorylation of histone H3 at serine 10. UVB distinctly increased Fyn kinase activity and phosphorylation. Fyn kinase inhibitors 4-amino-5-(4-chlorophenyl)-7(t-butyl)pyrazol(3,4-d)pyramide and leflunomide, an Src kinase inhibitor, suppressed both UVB-induced phosphorylation of histone H3 at serine 10 and Fyn kinase activity and phosphorylation. UVB-induced phosphorylation of histone H3 at serine 10 was blocked by either a dominant-negative mutant of Fyn (DNM-Fyn) kinase or small interfering RNA of Fyn kinase. UVB-induced phosphorylation and activities of ERKs and protein kinase B/Akt were markedly inhibited by DNM-Fyn kinase. However, DNM-Fyn kinase did not inhibit UVB-induced phosphorylation of p38 MAPK or c-Jun N-terminal kinases. Active Fyn kinase phosphorylated histone H3 at serine 10 in vitro, and the phosphorylated Fyn kinase could translocate into the nucleus of HaCaT cells. These results indicate that Fyn kinase plays a key role in the UVB-induced phosphorylation of histone H3 at serine 10.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>Dose-Response Relationship, Drug</subject><subject>Genes, Dominant</subject><subject>Histones - chemistry</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Isoxazoles - pharmacology</subject><subject>Leflunomide</subject><subject>MAP Kinase Signaling System</subject><subject>Mice</subject><subject>Models, Biological</subject><subject>p38 Mitogen-Activated Protein Kinases - metabolism</subject><subject>Phosphorylation</subject><subject>Plasmids - metabolism</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-akt</subject><subject>Proto-Oncogene Proteins c-fyn</subject><subject>RNA, Small Interfering - metabolism</subject><subject>Serine - chemistry</subject><subject>Serine - metabolism</subject><subject>Signal Transduction</subject><subject>src-Family Kinases - metabolism</subject><subject>Threonine - chemistry</subject><subject>Time Factors</subject><subject>Transfection</subject><subject>Ultraviolet Rays</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1r3DAQhkVpSTYf1x6L6KE3b0eyZcnHNjTZkISEpIEeCkKSZ2MFr7WV7JT991HYhT1lLsMMzwwvDyGfGcwZyOr7s3Xzmwo4iJIDfCAzBqosSsH-fCQzAM6Khgt1SI5SeoZcVcMOyCETopS14DPy9x6fpt6MPgw0LOljP0bz4kOPI_1Z-KGdHLb0rgtp3YW42YMLn8YwIF2U1Iz0AaPPAwNqN_R8M9ArP5iEJ-TT0vQJT3f9mDye__p9tiiuby8uz35cF05APRYSJEcrLLAG86K2qCRD1bq2RQdNaUXdSMkMYumsMFwCU2hq5MBrUFiXx-Tb9u86hn8TplGvfHLY92bAMCXNpGK8UlUG51vQxZBSxKVeR78ycaMZ6DefOvvUe5_54Mvu82RX2O7xncAMfN0CnX_q_vuI2vrgOlxprkBXmlfVWz61hTBLePEYdXIeh6w2H7hRt8G_F-AViduOAQ</recordid><startdate>20050128</startdate><enddate>20050128</enddate><creator>He, Zhiwei</creator><creator>Cho, Yong-Yeon</creator><creator>Ma, Wei-Ya</creator><creator>Choi, Hong Seok</creator><creator>Bode, Ann M.</creator><creator>Dong, Zigang</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20050128</creationdate><title>Regulation of Ultraviolet B-induced Phosphorylation of Histone H3 at Serine 10 by Fyn Kinase</title><author>He, Zhiwei ; Cho, Yong-Yeon ; Ma, Wei-Ya ; Choi, Hong Seok ; Bode, Ann M. ; Dong, Zigang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-7072eb5b019e5066be871e8dcddec093b569771aee3cb5a27018ea6e202608e63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Cell Line, Tumor</topic><topic>Dose-Response Relationship, Drug</topic><topic>Genes, Dominant</topic><topic>Histones - chemistry</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Isoxazoles - pharmacology</topic><topic>Leflunomide</topic><topic>MAP Kinase Signaling System</topic><topic>Mice</topic><topic>Models, Biological</topic><topic>p38 Mitogen-Activated Protein Kinases - metabolism</topic><topic>Phosphorylation</topic><topic>Plasmids - metabolism</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins c-akt</topic><topic>Proto-Oncogene Proteins c-fyn</topic><topic>RNA, Small Interfering - metabolism</topic><topic>Serine - chemistry</topic><topic>Serine - metabolism</topic><topic>Signal Transduction</topic><topic>src-Family Kinases - metabolism</topic><topic>Threonine - chemistry</topic><topic>Time Factors</topic><topic>Transfection</topic><topic>Ultraviolet Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>He, Zhiwei</creatorcontrib><creatorcontrib>Cho, Yong-Yeon</creatorcontrib><creatorcontrib>Ma, Wei-Ya</creatorcontrib><creatorcontrib>Choi, Hong Seok</creatorcontrib><creatorcontrib>Bode, Ann M.</creatorcontrib><creatorcontrib>Dong, Zigang</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>He, Zhiwei</au><au>Cho, Yong-Yeon</au><au>Ma, Wei-Ya</au><au>Choi, Hong Seok</au><au>Bode, Ann M.</au><au>Dong, Zigang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of Ultraviolet B-induced Phosphorylation of Histone H3 at Serine 10 by Fyn Kinase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2005-01-28</date><risdate>2005</risdate><volume>280</volume><issue>4</issue><spage>2446</spage><epage>2454</epage><pages>2446-2454</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Ultraviolet B (UVB) induces phosphorylation of histone H3 at serine 10, and mitogen-activated protein kinases are involved in this signal transduction pathway. Here we provide evidence that Fyn kinase, a member of the Src kinase family, is involved in the UVB-induced phosphorylation of histone H3 at serine 10. UVB distinctly increased Fyn kinase activity and phosphorylation. Fyn kinase inhibitors 4-amino-5-(4-chlorophenyl)-7(t-butyl)pyrazol(3,4-d)pyramide and leflunomide, an Src kinase inhibitor, suppressed both UVB-induced phosphorylation of histone H3 at serine 10 and Fyn kinase activity and phosphorylation. UVB-induced phosphorylation of histone H3 at serine 10 was blocked by either a dominant-negative mutant of Fyn (DNM-Fyn) kinase or small interfering RNA of Fyn kinase. UVB-induced phosphorylation and activities of ERKs and protein kinase B/Akt were markedly inhibited by DNM-Fyn kinase. However, DNM-Fyn kinase did not inhibit UVB-induced phosphorylation of p38 MAPK or c-Jun N-terminal kinases. Active Fyn kinase phosphorylated histone H3 at serine 10 in vitro, and the phosphorylated Fyn kinase could translocate into the nucleus of HaCaT cells. These results indicate that Fyn kinase plays a key role in the UVB-induced phosphorylation of histone H3 at serine 10.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15537652</pmid><doi>10.1074/jbc.M402053200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Cell Line Cell Line, Tumor Dose-Response Relationship, Drug Genes, Dominant Histones - chemistry Histones - metabolism Humans Isoxazoles - pharmacology Leflunomide MAP Kinase Signaling System Mice Models, Biological p38 Mitogen-Activated Protein Kinases - metabolism Phosphorylation Plasmids - metabolism Protein-Serine-Threonine Kinases - metabolism Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-akt Proto-Oncogene Proteins c-fyn RNA, Small Interfering - metabolism Serine - chemistry Serine - metabolism Signal Transduction src-Family Kinases - metabolism Threonine - chemistry Time Factors Transfection Ultraviolet Rays |
| title | Regulation of Ultraviolet B-induced Phosphorylation of Histone H3 at Serine 10 by Fyn Kinase |
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