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J Biol Chem, Vol. 274, Issue 2, 687-692, January 8, 1999
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From the A growing body of evidence indicates
that regulation of protein-serine/threonine phosphatase 2A (PP2A)
involves its association with other cellular and viral proteins in
multiprotein complexes. PP2A-containing protein complexes may exist
that contribute to PP2A's important regulatory role in many cellular
processes. To identify such protein complexes, PP2A was partially
purified from rat brain soluble extracts following treatment with a
reversible cross-linker to stabilize large molecular size forms of
PP2A. Compared with native (uncross-linked) PP2A, cross-linked PP2A revealed an enrichment of p70 S6 kinase and two p21-activated kinases
(PAK1 and PAK3) in the PP2A complex, indicating these kinases may
associate with PP2A. The existence of protein kinase-PP2A complexes in
rat brain soluble extracts was further substantiated by the following
results: 1) independent immunoprecipitation of the kinases revealed
that PP2A co-precipitated with p70 S6 kinase and the two PAK isoforms;
2) glutathione S-transferase fusion proteins of p70 S6
kinase and PAK3 each isolated PP2A; and 3) PAK3 and p70 S6 kinase bound
to microcystin-Sepharose (an affinity resin for PP2A-PP1).
Cumulatively, these findings provide evidence for association of PP2A
with p70 S6 kinase, PAK1, and PAK3 in the context of the cellular
environment. Moreover, together with the recent reports describing
associations of PP2A with
Ca2+/calmodulin-dependent protein kinase IV
(Westphal, R. S., Anderson, K. A., Means, A. R., and
Wadzinski, B. E. (1998) Science 280, 1258-1261) and
casein kinase II Department of Pharmacology, Vanderbilt
University School of Medicine, Nashville, Tennessee 37232-6600 and the
¶ Department of Medicine, University of British Columbia,
Vancouver, British Columbia V6T 1Z3, Canada
(Heriche, J. K., Lebrin, F., Rabilloud, T.,
Leroy, D., Chambaz, E. M., and Goldberg, Y. (1997) Science 276, 952-955), the present data provide compelling
evidence for the existence of protein kinase-PP2A signaling modules as a new paradigm for the control of various intracellular signaling cascades.
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