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Subunits of Protein Phosphatase 2A Direct the Enzyme to
Distinct Cellular Functions
(Received for publication, September 27, 1996, and in revised form, January 8, 1997)
From the Department of Biochemistry and Molecular Biology, Indiana
University School of Medicine, Indianapolis, Indiana 46202-5122 and the
§ Department of Biological Sciences, University at
Albany/State University of New York, Albany, New York 12222
Protein phosphatase 2A (PP2A) is a major cellular
serine/threonine protein phosphatase, present in the cell in a variety
of heterotrimeric forms that differ in their associated regulatory B-subunit. Cloning of the mammalian B
subunit has allowed the identification of a highly homologous Saccharomyces
cerevisiae gene, RTS1. Disruption of the gene results
in a temperature-sensitive growth defect that can be suppressed by
expression of rabbit B
or B
isoforms. The B subunit is much
more effective in restoring normal growth at 37 °C than B.
Immunoprecipitated Rts1p was found associated with type 2A-specific
protein phosphatase activity that is sensitive to 2 nM
okadaic acid, but not to 100 nM phosphatase inhibitor-2,
and to be phosphorylated in vivo. However, overexpression of RTS1 was unable to suppress the cold sensitivity,
defective cytokinesis, and abnormal cell morphology resulting from
defects in the CDC55 gene, which encodes the yeast homolog
of a different B subunit of another form of 2A phosphatase,
PP2A1. These results indicate that Rts1p is a yeast homolog
of the mammalian B subunit and that the various regulatory B-subunits
of PP2A are not functionally redundant but direct the enzyme to
distinct cellular functions.
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