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United States: American Society for Biochemistry and Molecular Biology
Erscheinungsjahr
2006
Link zum Volltext
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
Identification of protein-protein interactions is crucial for unraveling cellular processes and biochemical mechanisms of
signal transduction. Here we describe, for the first time, the application of the tandem affinity purification (TAP) and LC-MS
method to the characterization of protein complexes from transgenic mice. The TAP strategy developed in transgenic mice allows
the emplacement of complexes in their physiological environment in contact with proteins that might only be specifically expressed
in certain tissues while simultaneously ensuring the right stoichiometry of the TAP protein versus their binding partners and represents a novelty in proteomics approaches used so far. Mouse lines expressing TAP-tagged 14-3-3ζ
protein were generated, and protein interactions were determined. 14-3-3 proteins are general regulators of cell signaling
and represent up to 1% of the total brain protein. This study allowed the identification of almost 40 novel 14-3-3ζ-binding
proteins. Biochemical and functional characterization of some of these interactions revealed new mechanisms of action of 14-3-3ζ
in several signaling pathways, such as glutamate receptor signaling via binding to homer homolog 3 (Homer 3) and in cytoskeletal
rearrangements and spine morphogenesis by binding and regulating the activity of the signaling complex formed by G protein-coupled
receptor kinase-interactor 1 (GIT1) and p21-activated kinase-interacting exchange factor β (βPIX).