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J Biol Chem, Vol. 273, Issue 30, 19019-19024, July 24, 1998
From the Department of Molecular Microbiology and Immunology, K. Norris Jr. Comprehensive Cancer Center, University of Southern
California, Los Angeles, California 90033
Protein phosphatases are involved in many
cellular processes. One of the most abundant of these enzymes, the
serine/threonine-specific protein phosphatase type 2A (PP2A), is
present in most eukaryotic cells and serves a variety of functions.
However, the detailed study of its regulation and function has been
hampered by the difficulty of manipulating its expression level in cell
culture. By using a new mammalian expression vector to forcibly
overexpress PP2A in the mouse fibroblast cell line NIH3T3, we now show
that the catalytic subunit of PP2A is subject to a potent
autoregulatory mechanism that adjusts PP2A protein to constant levels.
This control is exerted at the translational level and does not involve
regulation of transcription or RNA processing. Thus, our results
demonstrate tight control of PP2A expression, and provide an
explanation for the difficulty of increasing PP2A expression
experimentally.
Autoregulation of Protein Phosphatase Type 2A Expression
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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