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Protein phosphatase 2A (PP-2A) is a heterotrimeric enzyme
consisting of a catalytic (C) subunit and A and B regulatory subunits.
PP-2A is activated by ceramide in vitro suggesting that PP-2A
may be a target of this putative second messenger in vivo (Dobrowsky, R. T., Kamibayashi, C., Mumby, M. C., and Hannun, Y.
A.(1993) J. Biol. Chem. 268, 15523-15530). In this study,
sensitivity to ceramide was only observed when the B subunit was
present, suggesting that the B subunit was required for ceramide
activation. Here we show that dimeric PP-2A, produced from trimeric
PP-2A by heparin-agarose-induced dissociation of the B subunit and
isolated by preparative native electrophoresis, is activated by
ceramide. The catalytic subunit of PP-2A, produced from trimeric PP-2A
by freezing and thawing in the presence of 0.2 M
Volume 270,
Number 21,
Issue of May 26, pp. 12808-12813, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-Ceramide
-mercaptoethanol and isolated by gel filtration, is also activated
by ceramide. The trimeric and catalytic subunit forms of PP-2A exhibit
a similar dose dependence of activation by ceramide, and are stimulated
to a similar extent at ceramide concentrations yielding maximal
activation. These findings indicate that neither the A nor the B
subunit is required for ceramide stimulation of PP-2A. Together, these
results demonstrate that the catalytic subunit contains a ceramide
binding site and suggest that efforts to understand the mechanism of
activation of PP-2A by ceramide should be focused on this subunit. The
discovery that the catalytic subunit contains a ceramide binding site
raises the possibility that other members of this serine/threonine
phosphatase gene family may contain lipid binding sites and be
regulated by ceramide or other lipid second messengers.
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