Caspases Disrupt the Nuclear-Cytoplasmic Barrier

doi:10.1083/jcb.151.5.951

Published online 20 November 2000. doi:10.1083/jcb.151.5.951

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© The Rockefeller University Press, 0021-9525/2000/11/951/ $5.00
The Journal of Cell Biology, Volume 151, Number 5, November 27, 2000 951-960

Original Article

Caspases Disrupt the Nuclear-Cytoplasmic Barrier

Lavina Faleiro^a,b and Yuri Lazebnik^a
^a Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724
^b Molecular and Cell Biology Graduate Program, State University of New York at Stony Brook, Stony Brook, New York 11733

Correspondence to: Yuri Lazebnik, Cold Spring Harbor Laboratory, One Bungtown Road, Cold Spring Harbor, NY 11724. Tel:(516) 367 8363 Fax:(516) 367 8461

During apoptosis, caspases, a family of proteases, disassemblea cell by cleaving a set of proteins. Caspase-3 plays a majorrole in the disassembly of the nucleus by processing severalnuclear substrates. The question is how caspase-3, which isusually cytoplasmic, gains access to its nuclear targets. Itwas suggested that caspase-3 is actively transported to thenucleus through the nuclear pores. We found that caspase-9,which is activated earlier than caspase-3, directly or indirectlyinactivates nuclear transport and increases the diffusion limitof the nuclear pores. This increase allows caspase-3 and othermolecules that could not pass through the nuclear pores in livingcells to enter or leave the nucleus during apoptosis by diffusion.Hence, caspase-9 contributes to cell disassembly by disruptingthe nuclear-cytoplasmic barrier.

Key Words: apoptosis, caspases, nuclear transport, nuclear pores

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