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First published online 6 May 2003
doi: 10.1242/jcs.00450
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Research Article |
and
of zebrafish: developmental expression and behavior during the cell cycle

1 Division of Electron Microscopy, Biocenter of the University of Wü
rzburg, Am Hubland, D-97074 Wü rzburg, Germany
2 Department of Biology, University of Ottawa, 30 Marie Curie, Ottawa, Ontario,
Canada K1N 6N5
3 Department of Biochemistry and Molecular Cell Biology, Vienna Biocenter,
University of Vienna, A-1030 Vienna, Austria
4 Department of Physiological Chemistry I, Biocenter of the University of
Wü rzburg, Am Hubland, D-97074 Wü rzburg, Germany
5 Ottawa Health Research Institute, 725 Parkdale Avenue, Ottawa, Ontario, Canada
K1Y 4E9
Author for correspondence (e-mail:
krohne{at}biozentrum.uni-wuerzburg.de)
Accepted 4 March 2003
Zebrafish lamina-associated polypeptides 2 (ZLAP2) ß,
and
have in common an N-terminal region with a LEM domain, and in the
C-terminal half of the molecule a lamina binding domain and a membrane
spanning sequence. The maternally synthesized
is the largest isoform
and the only LAP2 present in the rapidly dividing embryonic cells up to the
gastrula stage. ZLAP2
levels decrease during development, concomitant
with the increase of the somatic isoforms ZLAP2ß and
. In somatic
zebrafish cells ZLAP2
is the predominant isoform, whereas only small
amounts of ZLAP2ß are present.
During early embryonic development, ZLAP2
becomes associated with
mitotic chromosomes before anaphase. The surface of these chromosomes is
decorated with vesicles, and each chromosome assembles its own nuclear
envelope at the end of mitosis (karyomere formation). Ectopically expressed
ZLAP2
-green fluorescent protein (GFP) fusion protein targets vesicles
to mitotic chromosomes in Xenopus A6 cells, suggesting that
ZLAP2
is involved in karyomere formation during early zebrafish
development.
When ZLAP2ß and
were expressed as GFP fusion proteins in
Xenopus A6 cells, the ß- but not the
-isoform was found
in association with mitotic chromosomes, and ZLAP2ß-containing
chromosomes were decorated with vesicles. Further analysis of ZLAP2-GFP fusion
proteins containing only distinct domains of the ZLAP2 isoforms revealed that
the common N-terminal region in conjunction with ß- or
-specific
sequences mediate binding to mitotic chromosomes in vivo.
Key words: Zebrafish LAP2, Karyomere, Chromatin binding, Lamina, Mitosis
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