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(Received for publication, April 1, 1996, and in revised form, June 17, 1996)
From the Protein phosphatase 2A is a heterotrimeric
protein serine/threonine phosphatase consisting of a 36-kDa catalytic C
subunit, a 65-kDa structural A subunit, and a variable regulatory B
subunit. The B subunits determine the substrate specificity of the
enzyme. There have been three families of cellular B subunits
identified to date: B55, B56 (B
Volume 271, Number 36,
Issue of September 6, 1996
pp. 22081-22089
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,§
,§
Division of Molecular Biology and Genetics,
Department of Oncological Sciences, the § Program in Human
Molecular Biology and Genetics, the ¶ Combined Program in
Molecular Biology, and the 
Department of Pediatrics, University
of Utah School of Medicine, Salt Lake City, Utah 84112
), and PR72/130. We have now cloned
five genes encoding human B56 isoforms. Polypeptides encoded by all but
one splice variant (B56
1) are phosphoproteins, as shown by mobility
shift after treatment with alkaline phosphatase and metabolic labeling
with [32P]phosphate. All labeled isoforms contain solely
phosphoserine. Indirect immunofluorescence microscopy demonstrates
distinct patterns of intracellular targeting by different B56 isoforms.
Specifically, B56
, B56
, and B56
complexed with the protein
phosphatase 2A A and C subunits localize to the cytoplasm, whereas
B56
, B561, and B563 are concentrated in the nucleus. Two
isoforms (B56 and B56) are highly expressed in adult brain; here
we show that mRNA for these isoforms increases severalfold when
neuroblastoma cell lines are induced to differentiate by retinoic acid
treatment. These studies demonstrate an increasing diversity of
regulatory mechanisms to control the activity of this key intracellular
protein phosphatase and suggest distinct functions for isoforms
targeted to different intracellular locations.
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 W. Jiang and R. L. Hallberg Isolation and Characterization of par1+ and par2+: Two Schizosaccharomyces pombe Genes Encoding B' Subunits of Protein Phosphatase 2A Genetics, March 1, 2000; 154(3): 1025 - 1038. [Abstract] [Full Text]
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Y. Zhao, G. Boguslawski, R. S. Zitomer, and A. A. DePaoli-Roach Saccharomyces cerevisiae Homologs of Mammalian B and B' Subunits of Protein Phosphatase 2A Direct the Enzyme to Distinct Cellular Functions J. Biol. Chem., March 28, 1997; 272(13): 8256 - 8262. [Abstract] [Full Text] [PDF]
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M. J. Ratcliffe, K. Itoh, and S. Y. Sokol A Positive Role for the PP2A Catalytic Subunit in Wnt Signal Transduction J. Biol. Chem., November 10, 2000; 275(46): 35680 - 35683. [Abstract] [Full Text] [PDF]
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M. A. Davare, M. C. Horne, and J. W. Hell Protein Phosphatase 2A Is Associated with Class C L-type Calcium Channels (Cav1.2) and Antagonizes Channel Phosphorylation by cAMP-dependent Protein Kinase J. Biol. Chem., December 8, 2000; 275(50): 39710 - 39717. [Abstract] [Full Text] [PDF]
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H. Wei, D. G. Ashby, C. S. Moreno, E. Ogris, F. M. Yeong, A. H. Corbett, and D. C. Pallas Carboxymethylation of the PP2A Catalytic Subunit in Saccharomyces cerevisiae Is Required for Efficient Interaction with the B-type Subunits Cdc55p and Rts1p J. Biol. Chem., January 5, 2001; 276(2): 1570 - 1577. [Abstract] [Full Text] [PDF]
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H. Yamamoto, T. Hinoi, T. Michiue, A. Fukui, H. Usui, V. Janssens, C. Van Hoof, J. Goris, M. Asashima, and A. Kikuchi Inhibition of the Wnt Signaling Pathway by the PR61 Subunit of Protein Phosphatase 2A J. Biol. Chem., July 13, 2001; 276(29): 26875 - 26882. [Abstract] [Full Text] [PDF]
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A. Nishi, J. A. Bibb, G. L. Snyder, H. Higashi, A. C. Nairn, and P. Greengard Amplification of dopaminergic signaling by a positive feedback loop PNAS, November 7, 2000; 97(23): 12840 - 12845. [Abstract] [Full Text] [PDF]
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