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J. Biol. Chem., Vol. 277, Issue 21, 18898-18907, May 24, 2002
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From the Department of Biochemistry and Molecular Cell Biology,
Vienna Biocenter, University of Vienna, A-1030 Vienna, Austria
The non-membrane-bound
lamina-associated polypeptide 2 isoform, LAP2
Distinct Functions of the Unique C Terminus of LAP2
in
Cell Proliferation and Nuclear Assembly*
§,, and
, forms nucleoskeletal
structures with A-type lamins and interacts with chromosomes in a cell
cycle-dependent manner. LAP2 contains a LEM
(LAP2, emerin, and MAN1) domain in
the constant N terminus that binds to chromosomal
barrier-to-autointegration factor, and a C-terminal unique region that
is essential for chromosome binding. Here we show that C-terminal
LAP2 fragment efficiently bound to mitotic chromosomes and inhibited
assembly of endogenous LAP2, nuclear membranes, and lamins A/C in
in vitro nuclear assembly assays. Full-length recombinant
LAP2, which bound to chromosomes, and N-terminal fragment, which did
not bind, had no effect on assembly. This suggested an essential role
for the LAP2 C terminus in chromosome association and for the
N-terminal LEM domain in subsequent assembly stages. In
vivo analysis upon transient expression of GFP-tagged LAP2
fragments confirmed that, unlike the N-terminal fragment, the
C-terminal fragment was able to bind to chromosomes during mitosis, if
expressed weakly. At higher expression levels, C-terminal LAP2
fragment and full-length protein led to cell cycle arrest in interphase
and apoptosis, as shown by fluorescence-activated cell sorter analysis,
time lapse microscopy, and BrdUrd incorporation assays. These
data indicated distinct functions of LAP2 in cell cycle progression
during interphase and in nuclear reassembly during mitosis.
*
This study was supported by Grants P13374 and P15312 from
the Austrian Science Research Fund (to R. F.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contributed equally to this work.
§
A fellow in the International Ph.D. Program at the Vienna
Biocenter, supported by Grant WK001 from the Austrian Science Research Fund.
¶
To whom correspondence should be addressed: Dept. of
Biochemistry and Molecular Cell Biology, Vienna Biocenter, University of Vienna, Dr. Bohrgasse 9, A-1030 Vienna, Austria. Tel.:
43-1-4277-52856; Fax: 43-1-4277-52854; E-mail:
foisner@abc.univie.ac.at.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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