Structural and biochemical analysis of phosphorylation events during Wnt signal transduction

Placeholder Show Content

Abstract/Contents

Abstract
A great deal is known about elements of the Wnt signal transduction cascade and the [beta]-catenin destruction complex, but a complete molecular understanding of their function has remained elusive. Many of the proteins that are necessary for [beta]-catenin destruction, including GSK-3, CK1, Axin, and APC, also have roles in stabilizing [beta]-catenin on Wnt stimulation, thus confounding genetic analyses and cell culture overexpression studies in difficult-to-predict ways. In addition, Wnt signal transduction proteins such as GSK-3, CK1, and APC play critical roles in other signal transduction and metabolic cascades within cells, including such diverse pathways as glycogen regulation, circadian rhythm, spindle formation during mitosis, and microtubule stability. In order to carefully dissect Wnt signal transduction in the absence of these confounding factors, biochemical and structural studies were carried out on proteins from the destruction complex and the Wnt signaling cascade, with emphasis placed on the role of phosphorylation events on the APC, [beta]-catenin, and LRP5/6 proteins during the transition from [beta]-catenin destruction to activation.

Description

Type of resource text
Form electronic; electronic resource; remote
Extent 1 online resource.
Publication date 2013
Issuance monographic
Language English

Creators/Contributors

Associated with Stamos, Jennifer Lynn
Associated with Stanford University, Department of Molecular and Cellular Physiology.
Primary advisor Ferrell, James Ellsworth
Primary advisor Weis, William I
Thesis advisor Ferrell, James Ellsworth
Thesis advisor Weis, William I
Thesis advisor Jardetzky, Theodore
Thesis advisor Nusse, Roel, 1950-
Advisor Jardetzky, Theodore
Advisor Nusse, Roel, 1950-

Subjects

Genre Theses

Bibliographic information

Statement of responsibility Jennifer Lynn Stamos.
Note Submitted to the Department of Molecular and Cellular Physiology.
Thesis Ph.D. Stanford University 2013
Location electronic resource

Access conditions

Copyright
© 2013 by Jennifer Lynn Stamos
License
This work is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported license (CC BY-NC).

Also listed in

Loading usage metrics...