Glycobiology, 2002, Vol. 12, No. 5 329-337
© 2002 Oxford University Press
Shuttling of galectin-3 between the nucleus and cytoplasm
2 Cell and Molecular Biology Program, Michigan State University, East Lansing, MI 48824 USA; 3 Department of Microbiology, Michigan State University, East Lansing, MI 48824 USA; 4 INSERM 257, ICGM, Paris, France, 5 Institut Jacques Monod, 75251 Paris Cedex 05, France; and 6 Department of Biochemistry, Michigan State University, East Lansing, MI 48824 USA
In previous studies, we documented that galectin-3 (Mr ~ 30,000) is a pre-mRNA splicing factor. Recently, galectin-3 was identified as a component of a nuclear and cytoplasmic complex, the survival of motor neuron complex, through its interaction with Gemin4. To test the possibility that galectin-3 may shuttle between the nucleus and the cytoplasm, human fibroblasts (LG-1) were fused with mouse fibroblasts (3T3). The monoclonal antibody NCL-GAL3, which recognizes human galectin-3 but not the mouse homolog, was used to monitor the localization of human galectin-3 in heterodikaryons. Human galectin-3 localized to both nuclei of a large percentage of heterodikaryons. Addition of the antibiotic leptomycin B, which inhibits nuclear export of galectin-3, decreased the percentage of heterodikaryons showing human galectin-3 in both nuclei. In a parallel experiment, mouse 3T3 fibroblasts, which express galectin-3, were fused with fibroblasts derived from a mouse in which the galectin-3 gene was inactivated. Mouse galectin-3 localized to both nuclei of a large percentage of heterodikaryons. Again, addition of leptomycin B restricted the presence of galectin-3 to one nucleus of a heterodikaryon. The results from both heterodikaryon assays suggest that galectin-3 can exit one nucleus, travel through the cytoplasm, and enter the second nucleus, matching the definition of shuttling.
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