Regulation of recombinant PKCα activity by protein phosphatase 1 and protein phosphatase 2A
R Ricciarelli, A Azzi - Archives of biochemistry and biophysics, 1998 - Elsevier
R Ricciarelli, A Azzi
Archives of biochemistry and biophysics, 1998•ElsevierThe sensitivity of PKCα to two protein phosphatases (PP1and PP2A) has been studied. The
results show that both phosphatases reversibly inhibit PKCα activity suggesting an effect at
PKC autophosphorylation sites and not at transphosphorylation sites. Moreover, PP1has
been found at low concentration to activate PKCα implying the existence of an inhibitory
phosphorylation site. Further, PKCα has been shown to phosphorylate PP2A at its regulatory
subunit B.
results show that both phosphatases reversibly inhibit PKCα activity suggesting an effect at
PKC autophosphorylation sites and not at transphosphorylation sites. Moreover, PP1has
been found at low concentration to activate PKCα implying the existence of an inhibitory
phosphorylation site. Further, PKCα has been shown to phosphorylate PP2A at its regulatory
subunit B.
The sensitivity of PKCα to two protein phosphatases (PP1and PP2A) has been studied. The results show that both phosphatases reversibly inhibit PKCα activity suggesting an effect at PKC autophosphorylation sites and not at transphosphorylation sites. Moreover, PP1has been found at low concentration to activate PKCα implying the existence of an inhibitory phosphorylation site. Further, PKCα has been shown to phosphorylate PP2A at its regulatory subunit B.
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