KSR is a scaffold required for activation of the ERK/MAPK module
AUTOR(ES)
Roy, François
FONTE
Cold Spring Harbor Laboratory Press
RESUMO
Mechanisms that regulate signal propagation through the ERK/MAPK pathway are still poorly understood. Several proteins are suspected to play critical roles in this process. One of these is Kinase Suppressor of Ras (KSR), a component previously identified in RAS-dependent genetic screens in Drosophila and Caenorhabditis elegans. Here, we show that KSR functions upstream of MEK within the ERK/MAPK module. In agreement with this, we found that KSR facilitates the phosphorylation of MEK by RAF. We further show that KSR associates independently with RAF and MEK, and that these interactions lead to the formation of a RAF/MEK complex, thereby positioning RAF in close proximity to its substrate MEK. These findings suggest that KSR functions as a scaffold that assembles the RAF/MEK functional pair.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=155344Documentos Relacionados
- Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
- Participation of both Gab1 and Gab2 in the activation of the ERK/MAPK pathway by epidermal growth factor
- Identification and Functional Characterization of ERK/MAPK Phosphorylation Sites in the Runx2 Transcription Factor*
- Mixed lineage kinase-dependent JNK activation is governed by interactions of scaffold protein JIP with MAPK module components
- Kinase Suppressor of Ras (KSR) Is a Scaffold Which Facilitates Mitogen-Activated Protein Kinase Activation In Vivo