Abstract
The protein phosphatase 1 catalytic subunit (PP1c) and the protein phosphatase 2B (PP2B or calcineurin) catalytic subunit (CNA) contain nonconserved N‐terminal regions followed by conserved phosphatase cores. To examine the role of the N‐termini of these two phosphatases, we substituted the residues 1–8 of PP1c with residues 1–42 of CNA, which is designated CNA(1‐42)‐PP1(9‐330). The activities of CNA(1‐42)‐PP1(9‐330) were similar to those of PP2B and different from those of PP1. The chimera was at least fourfold less sensitive to inhibition by okadaic acid, but was stimulated by nickel ions and chlorogenic acid, characteristics of PP2B not of PP1. These observations suggest that the N‐terminus of CNA shifts the properties of PP1 toward those of PP2B. Our findings provide evidence that the nonconserved N‐terminus of PP2B not only functions as important regulatory domain but also confers itself particular characteristics. This region may be targeted for regulation of PP2B activities in vivo. © 2008 IUBMB IUBMB Life, 61(2): 178–183, 2009