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Vol. 13, Issue 9, 3138-3147, September 2002
and
Department of Cell and Molecular Biology, Feinberg School of
Medicine, Northwestern University, Chicago, Illinois 60611
The importin
family of nuclear-cytoplasmic transport factors
mediates the nuclear localization of proteins containing classical nuclear localization signals. Metazoan animals express multiple importin
proteins, suggesting their possible roles in cell
differentiation and development. Adult Caenorhabditis
elegans hermaphrodites express three importin
proteins,
IMA-1, IMA-2, and IMA-3, each with a distinct expression and
localization pattern. IMA-2 was expressed exclusively in germ line
cells from the early embryonic through adult stages. The protein has a
dynamic pattern of localization dependent on the stage of the cell
cycle. In interphase germ cells and embryonic cells, IMA-2 is
cytoplasmic and nuclear envelope associated, whereas in developing
oocytes, the protein is cytoplasmic and intranuclear. During mitosis in
germ line cells and embryos, IMA-2 surrounded the condensed chromosomes
but was not directly associated with the mitotic spindle. The timing of
IMA-2 nuclear localization suggested that the protein surrounded the
chromosomes after fenestration of the nuclear envelope in prometaphase.
Depletion of IMA-2 by RNA-mediated gene interference (RNAi) resulted in embryonic lethality and a terminal aneuploid phenotype.
ima-2(RNAi) embryos have severe defects in nuclear
envelope formation, accumulating nucleoporins and lamin in the
cytoplasm. We conclude that IMA-2 is required for proper chromosome
dynamics in germ line and early embryonic mitosis and is involved in
nuclear envelope assembly at the conclusion of mitosis.
Corresponding author. E-mail address:
s-adam{at}northwestern.edu.
Present addresses:
*Department of Molecular and Cell Biology, 401 Barker Hall, #3204, University of California, Berkeley, Berkeley, CA
94720-3204;
Akceli, Inc., 1 Hampshire St., Cambridge,
Massachusetts 02139.
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