Notch Signaling Suppresses p38 MAPK Activity via Induction of MKP-1 in Myogenesis
Cross-talks among intracellular signaling pathways are important for the regulation of cell fate decisions and cellular responses to extracellular signals. Both the Notch pathway and the MAPK pathways play important roles in many biological processes, and the Notch pathway has been shown to interact...
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| Veröffentlicht in: | The Journal of biological chemistry 2007-02, Vol.282 (5), p.3058-3065 |
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| container_end_page | 3065 |
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| container_title | The Journal of biological chemistry |
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| creator | Kondoh, Kunio Sunadome, Kazunori Nishida, Eisuke |
| description | Cross-talks among intracellular signaling pathways are important for the regulation of cell fate decisions and cellular responses to extracellular signals. Both the Notch pathway and the MAPK pathways play important roles in many biological processes, and the Notch pathway has been shown to interact with the ERK-type MAPK pathway. However, its interaction with the other MAPK pathways is unknown. Here we show that Notch signaling activation in C2C12 cells suppresses the activity of p38 MAPK to inhibit myogenesis. Our results show that Notch specifically induces expression of MKP-1, a member of the dual-specificity MAPK phosphatase, which directly inactivates p38 to negatively regulate C2C12 myogenesis. The Notch-induced expression of MKP-1 is shown to depend on RBP-J. Moreover, inhibition of MKP-1 expression by short interfering RNA suppresses p38 inactivation and partially rescues the negative regulation of myogenesis. These results reveal a novel cross-talk between the Notch pathway and the p38 MAPK pathway that is mediated by Notch induction of MKP-1. |
| doi_str_mv | 10.1074/jbc.M607630200 |
| format | Article |
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Both the Notch pathway and the MAPK pathways play important roles in many biological processes, and the Notch pathway has been shown to interact with the ERK-type MAPK pathway. However, its interaction with the other MAPK pathways is unknown. Here we show that Notch signaling activation in C2C12 cells suppresses the activity of p38 MAPK to inhibit myogenesis. Our results show that Notch specifically induces expression of MKP-1, a member of the dual-specificity MAPK phosphatase, which directly inactivates p38 to negatively regulate C2C12 myogenesis. The Notch-induced expression of MKP-1 is shown to depend on RBP-J. Moreover, inhibition of MKP-1 expression by short interfering RNA suppresses p38 inactivation and partially rescues the negative regulation of myogenesis. These results reveal a novel cross-talk between the Notch pathway and the p38 MAPK pathway that is mediated by Notch induction of MKP-1.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M607630200</identifier><identifier>PMID: 17158101</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cell Cycle Proteins - genetics ; Cell Line ; DNA, Complementary - genetics ; Dual Specificity Phosphatase 1 ; Enzyme Induction ; Genes, Reporter ; Immediate-Early Proteins - genetics ; Mice ; Muscle Development - physiology ; p38 Mitogen-Activated Protein Kinases - antagonists & inhibitors ; Phosphoprotein Phosphatases - genetics ; Plasmids ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases - genetics ; Receptors, Notch - antagonists & inhibitors ; Receptors, Notch - genetics ; Receptors, Notch - physiology ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - genetics ; Transfection</subject><ispartof>The Journal of biological chemistry, 2007-02, Vol.282 (5), p.3058-3065</ispartof><rights>2007 © 2007 ASBMB. 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Both the Notch pathway and the MAPK pathways play important roles in many biological processes, and the Notch pathway has been shown to interact with the ERK-type MAPK pathway. However, its interaction with the other MAPK pathways is unknown. Here we show that Notch signaling activation in C2C12 cells suppresses the activity of p38 MAPK to inhibit myogenesis. Our results show that Notch specifically induces expression of MKP-1, a member of the dual-specificity MAPK phosphatase, which directly inactivates p38 to negatively regulate C2C12 myogenesis. The Notch-induced expression of MKP-1 is shown to depend on RBP-J. Moreover, inhibition of MKP-1 expression by short interfering RNA suppresses p38 inactivation and partially rescues the negative regulation of myogenesis. These results reveal a novel cross-talk between the Notch pathway and the p38 MAPK pathway that is mediated by Notch induction of MKP-1.</description><subject>Animals</subject><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Line</subject><subject>DNA, Complementary - genetics</subject><subject>Dual Specificity Phosphatase 1</subject><subject>Enzyme Induction</subject><subject>Genes, Reporter</subject><subject>Immediate-Early Proteins - genetics</subject><subject>Mice</subject><subject>Muscle Development - physiology</subject><subject>p38 Mitogen-Activated Protein Kinases - antagonists & inhibitors</subject><subject>Phosphoprotein Phosphatases - genetics</subject><subject>Plasmids</subject><subject>Protein Phosphatase 1</subject><subject>Protein Tyrosine Phosphatases - genetics</subject><subject>Receptors, Notch - antagonists & inhibitors</subject><subject>Receptors, Notch - genetics</subject><subject>Receptors, Notch - physiology</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - genetics</subject><subject>Transfection</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1vEzEQhi0EoqH0yhGsHrhtGNu7XvsYVbRUbaAorcTNcvyxcZWsl_Vuqvx7XDZSTwhfRpaeeWfmQegDgTmBuvzyuDbzJYeaM6AAr9CMgGAFq8iv12gGQEkhaSVO0LuUHiG_UpK36ITUpBIEyAz9_B4Hs8Gr0LR6G9oGr8au611KLuGOCbxc3N3ghRnCPgwHvA8aX7d2zP_Y4ujx8uauIDi0eHmIjWtdCuk9euP1NrmzYz1FD5df7y--Fbc_rq4vFreFqUAOBa05YV4Lby2XgnppS8aBS211CVrWsrRUWrDG2FquqfHelbz0wJiw3FLGTtHnKbfr4-_RpUHtQjJuu9Wti2NSXMiqlFL8FySyYhXlMoPzCTR9TKl3XnV92On-oAioZ9sq21YvtnPDx2PyuN45-4If9WbgfAI2odk8hd6pdYhm43aKCqoqxaB63u_TBHkdlW76kNTDiuZuyCMJ_XuqmAiXfe6D61UywbXG2RxpBmVj-NeKfwAmSKBQ</recordid><startdate>20070202</startdate><enddate>20070202</enddate><creator>Kondoh, Kunio</creator><creator>Sunadome, Kazunori</creator><creator>Nishida, Eisuke</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</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><scope>7X8</scope></search><sort><creationdate>20070202</creationdate><title>Notch Signaling Suppresses p38 MAPK Activity via Induction of MKP-1 in Myogenesis</title><author>Kondoh, Kunio ; Sunadome, Kazunori ; Nishida, Eisuke</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c509t-27613fa8fdd6982f9d436069ada40a9794d29d0dccd79b2cffe464f0338d6d233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Cell Cycle Proteins - genetics</topic><topic>Cell Line</topic><topic>DNA, Complementary - genetics</topic><topic>Dual Specificity Phosphatase 1</topic><topic>Enzyme Induction</topic><topic>Genes, Reporter</topic><topic>Immediate-Early Proteins - genetics</topic><topic>Mice</topic><topic>Muscle Development - physiology</topic><topic>p38 Mitogen-Activated Protein Kinases - antagonists & inhibitors</topic><topic>Phosphoprotein Phosphatases - genetics</topic><topic>Plasmids</topic><topic>Protein Phosphatase 1</topic><topic>Protein Tyrosine Phosphatases - genetics</topic><topic>Receptors, Notch - antagonists & inhibitors</topic><topic>Receptors, Notch - genetics</topic><topic>Receptors, Notch - physiology</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - genetics</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kondoh, Kunio</creatorcontrib><creatorcontrib>Sunadome, Kazunori</creatorcontrib><creatorcontrib>Nishida, Eisuke</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</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><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kondoh, Kunio</au><au>Sunadome, Kazunori</au><au>Nishida, Eisuke</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Notch Signaling Suppresses p38 MAPK Activity via Induction of MKP-1 in Myogenesis</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2007-02-02</date><risdate>2007</risdate><volume>282</volume><issue>5</issue><spage>3058</spage><epage>3065</epage><pages>3058-3065</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Cross-talks among intracellular signaling pathways are important for the regulation of cell fate decisions and cellular responses to extracellular signals. Both the Notch pathway and the MAPK pathways play important roles in many biological processes, and the Notch pathway has been shown to interact with the ERK-type MAPK pathway. However, its interaction with the other MAPK pathways is unknown. Here we show that Notch signaling activation in C2C12 cells suppresses the activity of p38 MAPK to inhibit myogenesis. Our results show that Notch specifically induces expression of MKP-1, a member of the dual-specificity MAPK phosphatase, which directly inactivates p38 to negatively regulate C2C12 myogenesis. The Notch-induced expression of MKP-1 is shown to depend on RBP-J. Moreover, inhibition of MKP-1 expression by short interfering RNA suppresses p38 inactivation and partially rescues the negative regulation of myogenesis. 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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals Cell Cycle Proteins - genetics Cell Line DNA, Complementary - genetics Dual Specificity Phosphatase 1 Enzyme Induction Genes, Reporter Immediate-Early Proteins - genetics Mice Muscle Development - physiology p38 Mitogen-Activated Protein Kinases - antagonists & inhibitors Phosphoprotein Phosphatases - genetics Plasmids Protein Phosphatase 1 Protein Tyrosine Phosphatases - genetics Receptors, Notch - antagonists & inhibitors Receptors, Notch - genetics Receptors, Notch - physiology Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - genetics Transfection |
| title | Notch Signaling Suppresses p38 MAPK Activity via Induction of MKP-1 in Myogenesis |
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