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J. Biol. Chem., Vol. 269, Issue 51, 32214-32220, 12, 1994
W Wen, AT Harootunian, SR Adams, J Feramisco, RY Tsien, JL Meinkoth and SS Taylor
The heat-stable inhibitor of cAMP-dependent protein kinase (PKI) was shown
previously to export the kinase catalytic subunit (C) from the nucleus
(Fantozzi, D. A., Harootunian, A. T., Wen, W., Taylor, S. S., Feramisco,
J.R., Tsien, R. Y., and Meinkoth, J. L. (1994) J. Biol. Chem. 269,
2676-2686), in addition to its ability to inhibit kinase activity. In this
study, the mechanism of PKI export is investigated. The injection of a
C-PKI complex containing both labeled PKI and C- subunit revealed that both
proteins exit the nucleus in unison. A fusion protein of C-subunit with
glutathione S-transferase (GST) (140 kDa) cannot transverse the nuclear
membrane in either direction, but can be exported from the nucleus when
complexed with PKI, supporting the presence of a nuclear export signal
(NES) in the C-PKI complex. Fusions of PKI alpha with GST (70 kDa) or PKI
beta 1 with maltose- binding protein (MBP) (50 kDa) remain effective at
exporting complexes with C-subunit. The export of C-PKI is also sensitive
to temperature and energy depletion. Taken together, these results
demonstrate that export is both energy- and temperature-dependent, but
size-independent, consistent with an active signal-mediated export process.
GST-PKI exits from the nucleus even in the absence of C-subunit, indicating
that the NES resides entirely on PKI, but suggesting that fusion of PKI to
GST leads to a conformational change that mimics the exposure of the NES
caused by the binding of C. Since both PKI alpha and PKI beta 1 can export
C-subunit, the predicted export signal is likely to reside on the residues
conserved between PKI alpha and PKI beta 1.
Heat-stable inhibitors of cAMP-dependent protein kinase carry a nuclear export signal
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0654.
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