PHLPP1 and 2 also dephosphorylate the hydrophobic motifs of two classes of the protein kinase C (PKC) family: the conventional PKCs and the novel PKCs.  (The third class of PKCs, known as the atypicals, have a  phospho-mimetic at the hydrophobic motif, rendering them insensitive to PHLPP.)
The PKC family of kinases consists of 10 isoforms, whose sensitivity to various second messengers is dictated by their domain structure. The conventional PKCs can be activated by calcium and diacylglycerol, two important mediators of G protein-coupled receptor signaling.  The novel PKCs are activated by diacylglycerol but not calcium, while the atypical PKCs are activated by neither.
The PKC family, like Akt, plays roles in cell survival and motility.  Most PKC isoforms are anti-apoptotic, although PKCδ (a novel PKC isoform) is pro-apoptotic in some systems.
Although PKC possesses the same phosphorylation sites as Akt, its regulation is quite different.  PKC is constitutively phosphorylated, and its acute activity is regulated by binding of the enzyme to membranes.  Dephosphorylation of PKC at the hydrophobic motif by PHLPP allows PKC to be dephosphorylated at two other sites (the activation loop and the turn motif).  This in turn renders PKC sensitive to degradation.  Thus, prolonged increases in PHLPP expression or activity inhibit PKC phosphorylation and stability, decreasing the total levels of PKC over time.