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J. Biol. Chem., Vol. 269, Issue 31, 20139-20148, 08, 1994
C Kamibayashi, R Estes, RL Lickteig, SI Yang, C Craft and MC Mumby
Protein phosphatase 2A (PP2A) is composed of structural (A), catalytic (C),
and regulatory subunits (B). Immunological analyses identified B alpha/PR55
alpha as the major regulatory subunit of brain PP2A while a unique B'
subunit was associated with the cardiac enzyme. Recombinant PP2A
heterotrimers were purified from insect cells infected with baculoviruses
expressing A and C, in combination with viruses expressing B alpha/PR55
alpha, B beta/PR55 beta, or SV40 small tumor antigen (st). Phosphatase
activities of rAC-B alpha and rAC-B beta were similar to those for brain
AC-B alpha, while rAC-st was 50-80% less active. Heparin had no effect on
rAC-st myosin light chain phosphatase activity, while the B
subunit-containing forms were stimulated 2-3- fold. Protamine caused a
3-4-fold increase in AC-B alpha and rAC-st activities and a marked
activation of rAC-B beta (6-fold) and AC-B' (10.5-fold). When histone H1
was used as substrate, all of the heterotrimers were stimulated
approximately 4-fold by heparin. The activity of AC-B' and rAC-B beta were
increased 2-fold by Mn2+, while a 6-fold stimulation was observed with
rAC-st. Chemical cross-linking of AC-B alpha and AC-B beta generated
200-kDa complexes, while AC-st was present as a 150-kDa complex. These
results demonstrate that different regulatory proteins affect enzyme
activity and the response to agents that modify PP2A activity in vitro.
Different PP2A heterotrimers are likely to have distinct functions in vivo,
and changes in subunit composition will have an important impact on signal
transduction pathways.
Comparison of heterotrimeric protein phosphatase 2A containing different B subunits
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235-9041.
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A. M. Silverstein, C. A. Barrow, A. J. Davis, and M. C. Mumby Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits PNAS, April 2, 2002; 99(7): 4221 - 4226. [Abstract] [Full Text] [PDF]
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