A mammalian scaffold complex that selectively mediates MAP kinase activation
| dc.contributor.author | Whitmarsh, Alan J. | |
| dc.contributor.author | Cavanagh, Julie | |
| dc.contributor.author | Tournier, Cathy | |
| dc.contributor.author | Yasuda, Jun | |
| dc.contributor.author | Davis, Roger J. | |
| dc.date | 2022-08-11T08:09:35.000 | |
| dc.date.accessioned | 2022-08-23T16:36:30Z | |
| dc.date.available | 2022-08-23T16:36:30Z | |
| dc.date.issued | 1998-09-11 | |
| dc.date.submitted | 2009-03-31 | |
| dc.identifier.citation | <p>Science. 1998 Sep 11;281(5383):1671-4.</p> | |
| dc.identifier.issn | 0036-8075 (Print) | |
| dc.identifier.doi | 10.1126/science.281.5383.1671 | |
| dc.identifier.pmid | 9733513 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.14038/38800 | |
| dc.description.abstract | The c-Jun NH2-terminal kinase (JNK) group of mitogen-activated protein (MAP) kinases is activated by the exposure of cells to multiple forms of stress. A putative scaffold protein was identified that interacts with multiple components of the JNK signaling pathway, including the mixed-lineage group of MAP kinase kinase kinases (MLK), the MAP kinase kinase MKK7, and the MAP kinase JNK. This scaffold protein selectively enhanced JNK activation by the MLK signaling pathway. These data establish that a mammalian scaffold protein can mediate activation of a MAP kinase signaling pathway. | |
| dc.language.iso | en_US | |
| dc.relation | <p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9733513&dopt=Abstract">Link to Article in PubMed</a></p> | |
| dc.relation.url | https://doi.org/10.1126/science.281.5383.1671 | |
| dc.subject | Animals | |
| dc.subject | COS Cells | |
| dc.subject | Calcium-Calmodulin-Dependent Protein Kinases | |
| dc.subject | Carrier Proteins | |
| dc.subject | Cell Line | |
| dc.subject | Cercopithecus aethiops | |
| dc.subject | Enzyme Activation | |
| dc.subject | Interleukin-1 | |
| dc.subject | JNK Mitogen-Activated Protein Kinases | |
| dc.subject | MAP Kinase Kinase 7 | |
| dc.subject | *MAP Kinase Kinase Kinases | |
| dc.subject | *Mitogen-Activated Protein Kinase Kinases | |
| dc.subject | *Mitogen-Activated Protein Kinases | |
| dc.subject | Molecular Sequence Data | |
| dc.subject | Protein Kinases | |
| dc.subject | Protein-Serine-Threonine Kinases | |
| dc.subject | Recombinant Fusion Proteins | |
| dc.subject | *Signal Transduction | |
| dc.subject | Life Sciences | |
| dc.subject | Medicine and Health Sciences | |
| dc.title | A mammalian scaffold complex that selectively mediates MAP kinase activation | |
| dc.type | Journal Article | |
| dc.source.journaltitle | Science (New York, N.Y.) | |
| dc.source.volume | 281 | |
| dc.source.issue | 5383 | |
| dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/oapubs/1644 | |
| dc.identifier.contextkey | 805465 | |
| html.description.abstract | <p>The c-Jun NH2-terminal kinase (JNK) group of mitogen-activated protein (MAP) kinases is activated by the exposure of cells to multiple forms of stress. A putative scaffold protein was identified that interacts with multiple components of the JNK signaling pathway, including the mixed-lineage group of MAP kinase kinase kinases (MLK), the MAP kinase kinase MKK7, and the MAP kinase JNK. This scaffold protein selectively enhanced JNK activation by the MLK signaling pathway. These data establish that a mammalian scaffold protein can mediate activation of a MAP kinase signaling pathway.</p> | |
| dc.identifier.submissionpath | oapubs/1644 | |
| dc.contributor.department | Howard Hughes Medical Institute | |
| dc.contributor.department | Program in Molecular Medicine | |
| dc.source.pages | 1671-4 |
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Role of the JIP4 scaffold protein in the regulation of mitogen-activated protein kinase signaling pathwaysThe c-Jun NH2-terminal kinase (JNK)-interacting protein (JIP) group of scaffold proteins (JIP1, JIP2, and JIP3) can interact with components of the JNK signaling pathway and potently activate JNK. Here we describe the identification of a fourth member of the JIP family. The primary sequence of JIP4 is most closely related to that of JIP3. Like other members of the JIP family of scaffold proteins, JIP4 binds JNK and also the light chain of the microtubule motor protein kinesin-1. However, the function of JIP4 appears to be markedly different from other JIP proteins. Specifically, JIP4 does not activate JNK signaling. In contrast, JIP4 serves as an activator of the p38 mitogen-activated protein (MAP) kinase pathway by a mechanism that requires the MAP kinase kinases MKK3 and MKK6. The JIP4 scaffold protein therefore appears to be a new component of the p38 MAP kinase signaling pathway.
