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Perspectives
Interfering with MAP Kinase Docking Interactions: Implications and Perspectives for the p38 Route
Federico Mayor, Jr., Maria Jurado-Pueyo, Pedro M. Campos and Cristina Murga
volume 6 | issue 5
1 March 2007Pages: 528 - 533
This is an open-access article
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Docking interactions are key to understand the dynamic assembly of signal transduction complexes in the cell. In particular, the docking domain (D domain)-dependent interactions described so far for several MAPK routes are essential to specify the upstream regulators, downstream mediators and also inactivators that complex with the p38, JNK and ERK proteins. In addition to contributing to the maintenance of the linearity and specificity of these pathways, novel data have revealed that docking contacts also regulate the activity, subcellular distribution and substrate selection of each MAPK. Moreover, phosphorylation inside or around a docking domain is emerging as a novel mechanism of regulation of MAPK association with cellular partners, suggesting new potential strategies for the design of selective MAPK inhibitors. Here, we discuss these novel data and the biochemical and cellular implications they may have with specific emphasis on the p38 route.
Authors
Federico Mayor, Jr.
Departamento de Biología Molecular and Centro de Biología Molecular “SeveroOchoa”, Universidad Autónoma de Madrid; Madrid, Spain.
Maria Jurado-Pueyo
Departamento de Biología Molecular and Centro de Biología Molecular “SeveroOchoa”, Universidad Autónoma de Madrid; Madrid, Spain.
Pedro M. Campos
Departamento de Biología Molecular and Centro de Biología Molecular “SeveroOchoa”, Universidad Autónoma de Madrid; Madrid, Spain.
Cristina Murga
Departamento de Biología Molecular and Centro de Biología Molecular “SeveroOchoa”, Universidad Autónoma de Madrid; Madrid, Spain.
This is an open-access article
Download PDFIf the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.