PMID- 10569247
OWN - NLM
STAT- MEDLINE
DCOM- 19991222
LR  - 20101118
IS  - 0171-9335 (Print)
IS  - 0171-9335 (Linking)
VI  - 78
IP  - 10
DP  - 1999 Oct
TI  - Distribution of emerin during the cell cycle.
PG  - 749-56
AB  - Human emerin is a nuclear membrane protein that is lost or altered in patients
      with Emery-Dreifuss muscular dystrophy (EMD). While the protein is expressed 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 immunoblotting in the nuclear envelope of all
      vertebrates studied from man to Xenopus. Immunolocalizations and nuclear envelope
      extraction experiments confirm 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 complexes. 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 sublethal doses of the antimitotic drug
      vinblastine sulfate and found that emerin is present in the nuclear envelope, but
      is absent from AL. In contrast to the homogeneous distribution of emerin in the
      nuclear envelope of interphase cells, this protein shows a focal accumulation in 
      the nuclear membranes of late telophase cells. During early reassembly of the
      nuclear 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
      concentrated in areas of the mitotic spindle and in the midbody of mitotic cells 
      suggesting a close interaction of these proteins. Our data suggest that emerin
      participates in the reorganisation of the nuclear envelope at the end of mitosis.
FAU - Dabauvalle, M C
AU  - Dabauvalle MC
AD  - Department of Cell and Developmental Biology, Biocenter of the University of
      Wurzburg, Germany. med@biozentrum.uni-wuerz-burg.de
FAU - Muller, E
AU  - Muller E
FAU - Ewald, A
AU  - Ewald A
FAU - Kress, W
AU  - Kress W
FAU - Krohne, G
AU  - Krohne G
FAU - Muller, C R
AU  - Muller CR
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Eur J Cell Biol
JT  - European journal of cell biology
JID - 7906240
RN  - 0 (Membrane Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Thymopoietins)
RN  - 0 (emerin)
SB  - IM
MH  - Animals
MH  - Biological Evolution
MH  - Cell Cycle/*physiology
MH  - Cell Line
MH  - Cricetinae
MH  - Humans
MH  - Macropodidae
MH  - Membrane Proteins/*metabolism
MH  - Mice
MH  - Microscopy, Fluorescence
MH  - Mitosis/physiology
MH  - Muscular Dystrophies/metabolism
MH  - Nuclear Envelope/metabolism
MH  - Nuclear Proteins
MH  - Rats
MH  - Thymopoietins/*metabolism
MH  - Xenopus laevis
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - S0171-9335(99)80043-0 [pii]
AID - 10.1016/S0171-9335(99)80043-0 [doi]
PST - ppublish
SO  - Eur J Cell Biol. 1999 Oct;78(10):749-56. doi: 10.1016/S0171-9335(99)80043-0.