Analysis Biomolecular Interactions of PP1α (7-300) with Phactr1 (517-580) by BLI (CAT#: STEM-MB-0208-CJ)

Introduction

PPP family phosphatases are metalloenzymes that carry out the majority of protein serine/threonine dephosphorylation. The three Protein Phosphatase 1 (PP1) isoforms regulate diverse cellular processes, acting in partnership with over 200 different PP1-interacting proteins (PIPs). Some PIPs are PP1 substrates, but others are PP1 cofactors, which variously determine substrate specificity, subcellular targeting and/or coupling to regulatory pathways. PIPs can interact both with these grooves and with other PP1 surface features.

The four Phosphatase and actin regulator (Phactr) proteins are novel PIPs that are implicated in cytoskeletal regulation in animal models and cell culture settings. The Phactrs bind G-actin via multiple RPEL motifs present in their conserved N- and C-terminal regions. Phactr1 and Phactr3 inhibit dephosphorylation of phosphorylase a by PP1 in vitro, but Phactr4/PP1 complex formation is associated with cofilin dephosphorylation in vivo.