WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A.

Protein phosphatase 2A (PP2A) is a multifunctional serine/threonine phosphatase that is critical to many cellular processes including development, neuronal signaling, cell cycle regulation, and viral transformation. PP2A has been implicated in Ca(2+)-dependent signaling pathways, but how PP2A is targeted to these pathways is not understood. We have identified two calmodulin ...
(CaM)-binding proteins that form stable complexes with the PP2A A/C heterodimer and may represent a novel family of PP2A B-type subunits. These two proteins, striatin and S/G(2) nuclear autoantigen (SG2NA), are highly related WD40 repeat proteins of previously unknown function and distinct subcellular localizations. Striatin has been reported to associate with the post-synaptic densities of neurons, whereas SG2NA has been reported to be a nuclear protein expressed primarily during the S and G(2) phases of the cell cycle. We show that SG2NA, like striatin, binds to CaM in a Ca(2+)-dependent manner. In addition to CaM and PP2A, several unidentified proteins stably associate with the striatin-PP2A and SG2NA-PP2A complexes. Thus, one mechanism of targeting and organizing PP2A with components of Ca(2+)-dependent signaling pathways may be through the molecular scaffolding proteins striatin and SG2NA.
Mesh Terms:
3T3 Cells, Amino Acid Sequence, Animals, Autoantigens, Calcium, Calmodulin-Binding Proteins, Conserved Sequence, Epitopes, Histones, Mass Spectrometry, Membrane Proteins, Methylation, Mice, Molecular Sequence Data, Nerve Tissue Proteins, Phosphoprotein Phosphatases, Phosphorylation, Precipitin Tests, Protein Binding, Protein Phosphatase 2, Sequence Homology, Amino Acid, Signal Transduction
J. Biol. Chem.
Date: Feb. 25, 2000
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