Abstract
Protein Phosphatase 6 Subunit with Conserved Sit4-associated Protein Domain Targets IκBϵ
Highlights
An important biological role for PP6 in mammalian cells is indicated by its recent identification in a genome-wide screen for kinases and phosphatases that affect cell survival [25]
We demonstrate that these putative regulatory subunits associate with PP6 phosphatase compared with PP2A or PP4, and the SAPS domain itself is sufficient for recognition of PP6
The third arm of the tree includes multiple SAPS proteins in plants. Based on this phylogenetic analysis we propose that multiple Sit4-associated protein (SAP) proteins in S. cerevisiae converged to a single SAPS protein in S. pombe, C. elegans, and D. melanogaster, which diverged into multiple SAPS proteins in plants and vertebrates
Summary
An important biological role for PP6 in mammalian cells is indicated by its recent identification in a genome-wide screen for kinases and phosphatases that affect cell survival [25]. We report the identification of three human SAPS-related genes (called PP6R1, PP6R2, and PP6R3) and show the distinctive tissue distribution of the mRNA and expression of the proteins that differs from the mRNA distribution. Distribution of PP6 Protein in Tissues, Cells, and Subcellular Fractions—We produced and affinity-purified a specific PP6 antibody against a peptide corresponding to residues 292–305 at the extreme C terminus of the PP6 catalytic subunit.
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