Abstract
Mitogen-activated protein (MAP) kinases are proline-directed serine/threonine kinases that are activated by dual phosphorylation on threonine and tyrosine residues in response to a wide array of extracellular stimuli. Three distinct groups of MAP kinases have been identified in mammalian cells [extracellular-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38]. These MAP kinases are mediators of signal transduction from the cell surface to the nucleus. One nuclear target of these MAP kinase signaling pathways is the transcription factor AP-1. MAP kinases regulate AP-1 transcriptional activity by multiple mechanisms. Here we review recent progress towards understanding AP-1 regulation by the ERK, JNK, and p38 MAP kinase signal transduction pathways.
Original language | English |
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Pages (from-to) | 589-607 |
Number of pages | 19 |
Journal | Journal of Molecular Medicine |
Volume | 74 |
Issue number | 10 |
Publication status | Published - Oct 1996 |
Keywords
- Animals
- Calcium-Calmodulin-Dependent Protein Kinases
- Humans
- Mammals
- Signal Transduction
- Transcription Factor AP-1