Ontology highlight
ABSTRACT:
SUBMITTER: Dougherty MK
PROVIDER: S-EPMC2737517 | biostudies-literature | 2009 Jun
REPOSITORIES: biostudies-literature
Dougherty Michele K MK Ritt Daniel A DA Zhou Ming M Specht Suzanne I SI Monson Daniel M DM Veenstra Timothy D TD Morrison Deborah K DK
Molecular cell 20090601 6
Protein scaffolds have emerged as important regulators of MAPK cascades, facilitating kinase activation and providing crucial spatio/temporal control to their signaling outputs. Using a proteomics approach to compare the binding partners of the two mammalian KSR scaffolds, we find that both KSR1 and KSR2 interact with the kinase components of the ERK cascade and have a common function in promoting RTK-mediated ERK signaling. Strikingly, we find that the protein phosphatase calcineurin selectivel ...[more]