Notch Interferes with the Scaffold Function of JNK-Interacting Protein 1 to Inhibit the JNK Signaling Pathway
The transmembrane protein Notch is cleaved by γ-secretase to yield an active form, Notch intracellular domain (Notch-IC), in response to the binding of ligands, such as Jagged. Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2005-10, Vol.102 (40), p.14308-14313 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Kim, Jin Woo Kim, Myung Jin Kim, Kwang Je Yun, Hee Jae Chae, Ji Soo Hwang, Sang Gil Chang, Tong-Shin Park, Hee-Sae Lee, Kang-Woo Han, Pyung-Lim Cho, Ssang-Goo Kim, Tae-Wan Choi, Eui-Ju Massagué, Joan |
| description | The transmembrane protein Notch is cleaved by γ-secretase to yield an active form, Notch intracellular domain (Notch-IC), in response to the binding of ligands, such as Jagged. Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic development as well as cell growth, differentiation, and survival. We now show that Notch1-IC suppresses the scaffold activity of c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP1) in the JNK signaling pathway. Notch1-IC physically associated with the JNK binding domain of JIP1 and thereby interfered with the interaction between JIP1 and JNK. JIP1 mediated the activation of JNK1 induced by glucose deprivation in mouse embryonic fibroblasts, and ectopic expression of Notch1-IC inhibited JNK activation and apoptosis triggered by glucose deprivation. Taken together, these findings suggest that Notch1-IC negatively regulates the JNK pathway by disrupting the scaffold function of JIP1. |
| doi_str_mv | 10.1073/pnas.0501600102 |
| format | Article |
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Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic development as well as cell growth, differentiation, and survival. We now show that Notch1-IC suppresses the scaffold activity of c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP1) in the JNK signaling pathway. Notch1-IC physically associated with the JNK binding domain of JIP1 and thereby interfered with the interaction between JIP1 and JNK. JIP1 mediated the activation of JNK1 induced by glucose deprivation in mouse embryonic fibroblasts, and ectopic expression of Notch1-IC inhibited JNK activation and apoptosis triggered by glucose deprivation. Taken together, these findings suggest that Notch1-IC negatively regulates the JNK pathway by disrupting the scaffold function of JIP1.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0501600102</identifier><identifier>PMID: 16179393</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Animals ; Antibodies ; Apoptosis ; Apoptosis - genetics ; Biological Sciences ; Calcium-Binding Proteins - metabolism ; Cell Line ; Cellular biology ; Cellular immunity ; Cultured cells ; Gene expression regulation ; Genetic Vectors - genetics ; Glucose ; Glucose - metabolism ; HEK293 cells ; Humans ; Immunoblotting ; Immunoprecipitation ; Intercellular Signaling Peptides and Proteins ; Jagged-1 Protein ; JNK Mitogen-Activated Protein Kinases - metabolism ; Luciferases ; Membrane Proteins - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Proteins ; Receptor, Notch1 - genetics ; Receptor, Notch1 - metabolism ; Scaffolds ; Serrate-Jagged Proteins ; Signal transduction ; Signal Transduction - physiology ; T lymphocytes</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2005-10, Vol.102 (40), p.14308-14313</ispartof><rights>Copyright 1993/2005 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Oct 4, 2005</rights><rights>Copyright © 2005, The National Academy of Sciences 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c498t-5fb9c5e1358e6defbc19ef6c682593364b8c27d25c3b43f1ec30b3e36303d8a73</citedby><cites>FETCH-LOGICAL-c498t-5fb9c5e1358e6defbc19ef6c682593364b8c27d25c3b43f1ec30b3e36303d8a73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/102/40.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3376735$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3376735$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16179393$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Jin Woo</creatorcontrib><creatorcontrib>Kim, Myung Jin</creatorcontrib><creatorcontrib>Kim, Kwang Je</creatorcontrib><creatorcontrib>Yun, Hee Jae</creatorcontrib><creatorcontrib>Chae, Ji Soo</creatorcontrib><creatorcontrib>Hwang, Sang Gil</creatorcontrib><creatorcontrib>Chang, Tong-Shin</creatorcontrib><creatorcontrib>Park, Hee-Sae</creatorcontrib><creatorcontrib>Lee, Kang-Woo</creatorcontrib><creatorcontrib>Han, Pyung-Lim</creatorcontrib><creatorcontrib>Cho, Ssang-Goo</creatorcontrib><creatorcontrib>Kim, Tae-Wan</creatorcontrib><creatorcontrib>Choi, Eui-Ju</creatorcontrib><creatorcontrib>Massagué, Joan</creatorcontrib><title>Notch Interferes with the Scaffold Function of JNK-Interacting Protein 1 to Inhibit the JNK Signaling Pathway</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The transmembrane protein Notch is cleaved by γ-secretase to yield an active form, Notch intracellular domain (Notch-IC), in response to the binding of ligands, such as Jagged. Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic development as well as cell growth, differentiation, and survival. We now show that Notch1-IC suppresses the scaffold activity of c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP1) in the JNK signaling pathway. Notch1-IC physically associated with the JNK binding domain of JIP1 and thereby interfered with the interaction between JIP1 and JNK. JIP1 mediated the activation of JNK1 induced by glucose deprivation in mouse embryonic fibroblasts, and ectopic expression of Notch1-IC inhibited JNK activation and apoptosis triggered by glucose deprivation. Taken together, these findings suggest that Notch1-IC negatively regulates the JNK pathway by disrupting the scaffold function of JIP1.</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Apoptosis</subject><subject>Apoptosis - genetics</subject><subject>Biological Sciences</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cellular biology</subject><subject>Cellular immunity</subject><subject>Cultured cells</subject><subject>Gene expression regulation</subject><subject>Genetic Vectors - genetics</subject><subject>Glucose</subject><subject>Glucose - metabolism</subject><subject>HEK293 cells</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Immunoprecipitation</subject><subject>Intercellular Signaling Peptides and Proteins</subject><subject>Jagged-1 Protein</subject><subject>JNK Mitogen-Activated Protein Kinases - metabolism</subject><subject>Luciferases</subject><subject>Membrane Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Receptor, Notch1 - genetics</subject><subject>Receptor, Notch1 - metabolism</subject><subject>Scaffolds</subject><subject>Serrate-Jagged Proteins</subject><subject>Signal transduction</subject><subject>Signal Transduction - physiology</subject><subject>T lymphocytes</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c1rFDEYBvBBLHatnr2IBA-Ch2nffE7mIkixtlqqUD2HTDbZyTI7WZOMtf-92Q-66sVTIPm9D3l5quoFhlMMDT1bjzqdAgcsADCQR9UMQ4trwVp4XM0ASFNLRthx9TSlJQC0XMKT6hgL3LS0pbNqdROy6dHVmG10NtqE7nzuUe4tujXauTDM0cU0muzDiIJDn24-11usy9W4QF9jyNaPCKMcSkrvO5-30wWiW78Y9bBlOvd3-v5ZdeT0kOzz_XlSfb_48O38sr7-8vHq_P11bVgrc81d1xpuMeXSirl1ncGtdcIISXhLqWCdNKSZE25ox6jD1lDoqKWCAp1L3dCT6t0udz11Kzs3dsxRD2od_UrHexW0V3-_jL5Xi_BTYcIIkVAC3uwDYvgx2ZTVyidjh0GPNkxJCSkaJhgp8PU_cBmmWLZOigAu_-GSF3S2QyaGlKJ1Dz_BoDY9qk2P6tBjmXj15wIHvy-uALQHm8lDHFGsRDIKspC3_yHKTcOQ7a9c7MudXaYc4gOmtBEN5fQ3cae7gw</recordid><startdate>20051004</startdate><enddate>20051004</enddate><creator>Kim, Jin Woo</creator><creator>Kim, Myung Jin</creator><creator>Kim, Kwang Je</creator><creator>Yun, Hee Jae</creator><creator>Chae, Ji Soo</creator><creator>Hwang, Sang Gil</creator><creator>Chang, Tong-Shin</creator><creator>Park, Hee-Sae</creator><creator>Lee, Kang-Woo</creator><creator>Han, Pyung-Lim</creator><creator>Cho, Ssang-Goo</creator><creator>Kim, Tae-Wan</creator><creator>Choi, Eui-Ju</creator><creator>Massagué, Joan</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20051004</creationdate><title>Notch Interferes with the Scaffold Function of JNK-Interacting Protein 1 to Inhibit the JNK Signaling Pathway</title><author>Kim, Jin Woo ; Kim, Myung Jin ; Kim, Kwang Je ; Yun, Hee Jae ; Chae, Ji Soo ; Hwang, Sang Gil ; Chang, Tong-Shin ; Park, Hee-Sae ; Lee, Kang-Woo ; Han, Pyung-Lim ; Cho, Ssang-Goo ; Kim, Tae-Wan ; Choi, Eui-Ju ; Massagué, Joan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c498t-5fb9c5e1358e6defbc19ef6c682593364b8c27d25c3b43f1ec30b3e36303d8a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Apoptosis</topic><topic>Apoptosis - genetics</topic><topic>Biological Sciences</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Cell Line</topic><topic>Cellular biology</topic><topic>Cellular immunity</topic><topic>Cultured cells</topic><topic>Gene expression regulation</topic><topic>Genetic Vectors - genetics</topic><topic>Glucose</topic><topic>Glucose - metabolism</topic><topic>HEK293 cells</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Immunoprecipitation</topic><topic>Intercellular Signaling Peptides and Proteins</topic><topic>Jagged-1 Protein</topic><topic>JNK Mitogen-Activated Protein Kinases - metabolism</topic><topic>Luciferases</topic><topic>Membrane Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Receptor, Notch1 - genetics</topic><topic>Receptor, Notch1 - metabolism</topic><topic>Scaffolds</topic><topic>Serrate-Jagged Proteins</topic><topic>Signal transduction</topic><topic>Signal Transduction - physiology</topic><topic>T lymphocytes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Jin Woo</creatorcontrib><creatorcontrib>Kim, Myung Jin</creatorcontrib><creatorcontrib>Kim, Kwang Je</creatorcontrib><creatorcontrib>Yun, Hee Jae</creatorcontrib><creatorcontrib>Chae, Ji Soo</creatorcontrib><creatorcontrib>Hwang, Sang Gil</creatorcontrib><creatorcontrib>Chang, Tong-Shin</creatorcontrib><creatorcontrib>Park, Hee-Sae</creatorcontrib><creatorcontrib>Lee, Kang-Woo</creatorcontrib><creatorcontrib>Han, Pyung-Lim</creatorcontrib><creatorcontrib>Cho, Ssang-Goo</creatorcontrib><creatorcontrib>Kim, Tae-Wan</creatorcontrib><creatorcontrib>Choi, Eui-Ju</creatorcontrib><creatorcontrib>Massagué, Joan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Jin Woo</au><au>Kim, Myung Jin</au><au>Kim, Kwang Je</au><au>Yun, Hee Jae</au><au>Chae, Ji Soo</au><au>Hwang, Sang Gil</au><au>Chang, Tong-Shin</au><au>Park, Hee-Sae</au><au>Lee, Kang-Woo</au><au>Han, Pyung-Lim</au><au>Cho, Ssang-Goo</au><au>Kim, Tae-Wan</au><au>Choi, Eui-Ju</au><au>Massagué, Joan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Notch Interferes with the Scaffold Function of JNK-Interacting Protein 1 to Inhibit the JNK Signaling Pathway</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2005-10-04</date><risdate>2005</risdate><volume>102</volume><issue>40</issue><spage>14308</spage><epage>14313</epage><pages>14308-14313</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The transmembrane protein Notch is cleaved by γ-secretase to yield an active form, Notch intracellular domain (Notch-IC), in response to the binding of ligands, such as Jagged. Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic development as well as cell growth, differentiation, and survival. We now show that Notch1-IC suppresses the scaffold activity of c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP1) in the JNK signaling pathway. Notch1-IC physically associated with the JNK binding domain of JIP1 and thereby interfered with the interaction between JIP1 and JNK. JIP1 mediated the activation of JNK1 induced by glucose deprivation in mouse embryonic fibroblasts, and ectopic expression of Notch1-IC inhibited JNK activation and apoptosis triggered by glucose deprivation. Taken together, these findings suggest that Notch1-IC negatively regulates the JNK pathway by disrupting the scaffold function of JIP1.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>16179393</pmid><doi>10.1073/pnas.0501600102</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing - metabolism Animals Antibodies Apoptosis Apoptosis - genetics Biological Sciences Calcium-Binding Proteins - metabolism Cell Line Cellular biology Cellular immunity Cultured cells Gene expression regulation Genetic Vectors - genetics Glucose Glucose - metabolism HEK293 cells Humans Immunoblotting Immunoprecipitation Intercellular Signaling Peptides and Proteins Jagged-1 Protein JNK Mitogen-Activated Protein Kinases - metabolism Luciferases Membrane Proteins - metabolism Protein Binding Protein Structure, Tertiary Proteins Receptor, Notch1 - genetics Receptor, Notch1 - metabolism Scaffolds Serrate-Jagged Proteins Signal transduction Signal Transduction - physiology T lymphocytes |
| title | Notch Interferes with the Scaffold Function of JNK-Interacting Protein 1 to Inhibit the JNK Signaling Pathway |
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