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© The Rockefeller University Press,
0021-9525/2000//951 $5.00
The Journal of Cell Biology, Volume 151, Number 5,
, 2000 951-960
Original Article |
Caspases Disrupt the Nuclear-Cytoplasmic Barrier
During apoptosis, caspases, a family of proteases, disassemble a cell by cleaving a set of proteins. Caspase-3 plays a major role in the disassembly of the nucleus by processing several nuclear substrates. The question is how caspase-3, which is usually cytoplasmic, gains access to its nuclear targets. It was suggested that caspase-3 is actively transported to the nucleus through the nuclear pores. We found that caspase-9, which is activated earlier than caspase-3, directly or indirectly inactivates nuclear transport and increases the diffusion limit of the nuclear pores. This increase allows caspase-3 and other molecules that could not pass through the nuclear pores in living cells to enter or leave the nucleus during apoptosis by diffusion. Hence, caspase-9 contributes to cell disassembly by disrupting the nuclear-cytoplasmic barrier.
Key Words: apoptosis • caspases • nuclear transport • nuclear pores
© 2000 The Rockefeller University Press
Abbreviations used in this paper: C9DN, caspase-9 dominant-negative mutant; DAPI, 4'6-diamidino-2-phenylindole; GFP, green fluorescent protein; NLS, nuclear localization signal.
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