The Role of KSR-Associated Kinases in Breast Cancer Signaling
Abstract
Increased levels of ERK MAP kinases and increased MAP kinase activity have been demonstrated in malignant breast carcinomas. Therefore, regulators of MAP kinase activity are attractive targets for breast cancer therapeutic intervention. Kinase Suppressor of Ras (KSR) is a recently characterized component of a key signaling pathway that activates MAP kinases, the Ras/Raf/MAP kinase pathway. KSR appears to function as a scaffold protein, bringing together on a single platform many of the components involved in this signaling pathway for efficient signal transduction. KSR moves between different cellular compartments in response to extracellular growth signals. The phosphorylation state of KSR appears to play a significant role in determining its intracellular localization, which in turn affects its function. The goal of the current project is to identify specific kinases which bind to and phosphorylate KSR, thereby providing an opportunity to alter the phosphorylation state of KSR and its ability to function in the Pas/Raf/MAP kinase pathway. We have developed a method of purifying KSR-associated proteins which has yielded several candidate proteins that we are currently characterizing. These studies promise to yield valuable information regarding KSR function in breast cancer.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 2002
- Accession Number
- ADA401105
Entities
People
- Paul Beumr
Organizations
- University of Nebraska Medical Center