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J. Cell Biol.,
Volume 144, Number 2, January 25, 1999 225-240
* MRC Protein Phosphorylation Unit, In this work, we have used novel mAbs
against two proteins of the endoplasmic reticulum and
outer nuclear membrane, termed NEP-B78 and p65, in
addition to a polyclonal antibody against the inner nuclear membrane protein LBR (lamin B receptor), to study the order and dynamics of NE reassembly in the
Xenopus cell-free system. Using these reagents, we
demonstrate differences in the timing of recruitment of
their cognate membrane proteins to the surface of decondensing chromatin in both the cell-free system and
XLK-2 cells. We show unequivocally that, in the cell-free system, two functionally and biochemically distinct
vesicle types are necessary for NE assembly. We find
that the process of distinct vesicle recruitment to chromatin is an ordered one and that NEP-B78 defines a
vesicle population involved in the earliest events of reassembly in this system. Finally, we present evidence
that NEP-B78 may be required for the targeting of
these vesicles to the surface of decondensing chromatin
in this system. The results have important implications
for the understanding of the mechanisms of nuclear envelope disassembly and reassembly during mitosis and
for the development of systems to identify novel molecules that control these processes.
Department of Biochemistry, and § Department of Biological Sciences, University of
Dundee, Dundee DD1 4HN, Scotland, United Kingdom; and Paterson Institute for Cancer Research, Christie Hospital,
Manchester M20 4BX, United Kingdom
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