Human emerin is a nuclear membrane protein that is lost or altered in patie
nts with Emery-Dreifuss muscular dystrophy (EMD). While the protein is expr
essed in the majority of human tissues analyzed, the pathology predominates
in cardiac and skeletal muscles of patients with EMD.
Our results show that emerin can be detected by immunocytochemistry and imm
unoblotting in the nuclear envelope of all vertebrates studied from man to
Xenopus. Immunolocalizations and nuclear envelope extraction experiments co
nfirm that emerin possesses properties characteristic for integral membrane
proteins of the inner nuclear membrane.
Some nuclear envelope proteins are localized also in annulate lamellae (AL)
, i.e. cytoplasmic flattened membrane cisternae penetrated by pore complexe
s. To verify whether emerin is contained in these membrane stacks, we have
induced the formation of AL by exposure of rat cells (line RV-SMC) to suble
thal doses of the antimitotic drug vinblastine sulfate and found that emeri
n is present in the nuclear envelope, but is absent from AL.
In contrast to the homogeneous distribution of emerin in the nuclear envelo
pe of interphase cells, this protein shows a focal accumulation in the nucl
ear membranes of late telophase cells. During early reassembly of the nucle
ar envelope at this mitotic stage emerin colocalizes with lamin A/C but not
with lamin B and LAP2 proteins, Confocal! laser scanning microscopy after
double-labeling experiments with emerin and tubulin shows that emerin is co
ncentrated in areas of the mitotic spindle and in the midbody of mitotic ce
lls suggesting a close interaction of these proteins. Our data suggest that
emerin participates in the reorganisation of the nuclear envelope at the e
nd of mitosis.