The Role of Protein Phosphatase 2A Catalytic Subunit Cα in Embryogenesis: Evidence from Sequence Analysis and Localization Studies
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Jürgen Götz
Abstract
Protein phosphatase 2A (PP2A) constitutes one of the major families of protein serine/threonine phosphatases found in all eukaryotic cells. PP2A holoenzymes are composed of a catalytic subunit complexed with a structural regulatory subunit of 65 kDa. These core subunits associate with regulatory subunits of various sizes to form different heterotrimers which have been purified and evaluated with regard to substrate specificity. In fully differentiated tissues PP2A expression levels are highest in the brain, however, relatively little is known about expression in the developing embryo.
In order to determine the composition of PP2A catalytic subunits in the mouse, cDNAs were cloned and the genomic organization of PP2A Cα was determined.
By a gene targeting approach in the mouse, we have previously shown that the absence of the major catalytic subunit of PP2A, Cα, resulted in embryonic lethality around embryonic day E6.5. No mesoderm was formed which implied that PP2A plays a crucial role in gastrulation.
Here, we extended our studies and analyzed wildtype embryos for Cα expression at subsequent stages of development. After gastrulation is completed, we find high expression of Cα restricted to the neural folds, which suggests that PP2A plays an additional pivotal role in neurulation.
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
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- Execution of Apoptosis: Converging or Diverging Pathways?
- Two Highly Related Homeodomain Proteins, Nkx5-1 and Nkx5-2, Display Different DNA Binding Specificities
- The Janus Face of the Archaeal Cdc48/p97 Homologue VAT: Protein Folding versus Unfolding
- Functional Characterization of an Extremely Thermophilic ATPase in Membranes of the Crenarchaeon Acidianus ambivalens
- On the Lysosomal Degradation of Neurofibromin and Its Phosphorylation in Cultured Melanocytes
- Rat Muscle Fructose-1,6-Bisphosphatase: Cloning of the cDNA, Expression of the Recombinant Enzyme, and Expression Analysis in Different Tissues
- Catalase-Peroxidase from the Cyanobacterium Synechocystis PCC 6803: Cloning, Overexpression in Escherichia coli, and Kinetic Characterization
- Expression of Plasma Prekallikrein mRNA in Human Nonhepatic Tissues and Cell Lineages Suggests Special Local Functions of the Enzyme
- Biochemical Characterization of the Catalytic Domain of Membrane-Type 4 Matrix Metalloproteinase
- Fluorometric Microassays for the Determination of Cathepsin L and Cathepsin S Activities in Tissue Extracts
- The Role of Protein Phosphatase 2A Catalytic Subunit Cα in Embryogenesis: Evidence from Sequence Analysis and Localization Studies
- DNA Binding of Myc/Max/Mad Network Complexes to Oligonucleotides Containing Two E Box Elements: c-Myc/Max Heterodimers Do Not Bind DNA Cooperatively
- Tight Interaction between Densely Methylated DNA Fragments and the Methyl-CpG Binding Domain of the Rat MeCP2 Protein Attached to a Solid Support
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