14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport
A Brunet, F Kanai, J Stehn, J Xu, D Sarbassova… - Journal of Cell …, 2002 - rupress.org
Journal of Cell Biology, 2002•rupress.org
1 14-3-3, which had been proposed to function as a nuclear export signal (NES), instead
functions globally in ligand binding and does not directly mediate nuclear transport. Efficient
nuclear export of FKHRL1 requires both intrinsic NES sequences within FKHRL1 and
phosphorylation/14-3-3 binding. Finally, we present evidence that phosphorylation/14-3-3
binding may also prevent FKHRL1 nuclear reimport. These results indicate that 14-3-3 can
mediate the relocalization of nuclear ligands by several mechanisms that ensure complete …
functions globally in ligand binding and does not directly mediate nuclear transport. Efficient
nuclear export of FKHRL1 requires both intrinsic NES sequences within FKHRL1 and
phosphorylation/14-3-3 binding. Finally, we present evidence that phosphorylation/14-3-3
binding may also prevent FKHRL1 nuclear reimport. These results indicate that 14-3-3 can
mediate the relocalization of nuclear ligands by several mechanisms that ensure complete …
1
14-3-3, which had been proposed to function as a nuclear export signal (NES), instead functions globally in ligand binding and does not directly mediate nuclear transport. Efficient nuclear export of FKHRL1 requires both intrinsic NES sequences within FKHRL1 and phosphorylation/14-3-3 binding. Finally, we present evidence that phosphorylation/14-3-3 binding may also prevent FKHRL1 nuclear reimport. These results indicate that 14-3-3 can mediate the relocalization of nuclear ligands by several mechanisms that ensure complete sequestration of the bound 14-3-3 complex in the cytoplasm.
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