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Vol. 12, Issue 8, 2328-2340, August 2001
and
*Department of Molecular Cell Biology, The Weizmann Institute of
Science, Rehovot, Israel; The spatial nuclear organization of regulatory proteins often
reflects their functional state. PSF, a factor essential for pre-mRNA
splicing, is visualized by the B92 mAb as discrete nuclear foci, which
disappeared during apoptosis. Because this mode of cell death entails
protein degradation, it was considered that PSF, which like other
splicing factors is sensitive to proteolysis, might be degraded.
Nonetheless, during the apoptotic process, PSF remained intact and was
N-terminally hyperphosphorylated on serine and threonine residues.
Retarded gel migration profiles suggested differential phosphorylation
of the molecule in mitosis vs. apoptosis and under-phosphorylation
during blockage of cells at G1/S. Experiments with the use of
recombinant GFP-tagged PSF provided evidence that in the course of
apoptosis the antigenic epitopes of PSF are masked and that PSF
reorganizes into globular nuclear structures. In apoptotic cells, PSF
dissociated from PTB and bound new partners, including the U1-70K and
SR proteins and therefore may acquire new functions.
Department of Molecular
Biology, Vanderbilt University, Nashville, Tennessee; and
Department of Medical Protein Chemistry (VIB),
University of Ghent, Ghent, Belgium
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