The major residual structure that remains associated with
the nuclear envelope following extraction of isolated nuclei
or oocyte germinal vesicles with non-ionic detergents,
nucleases and high salt is the lamina (Fawcett, 1966;
Aaronson and Blobel, 1975; Dwyer and Blobel, 1976). The
nuclear lamina is composed of intermediate filament
proteins, termed lamins (Gerace and Blobel, 1980; Shelton
et al., 1980), which polymerise to form a basket-weave
lattice of fibrils, which covers the entire inner surface of the
nuclear envelope and interlinks nuclear pores (Aebi et al.,
1986; Stewart and Whytock, 1988; Goldberg and Allen,
1992). At mitosis, the nuclear envelope and the lamina both
break down to allow chromosome segregation. As a consequence,
each structure has to be rebuilt during anaphase
and telophase, allowing cells an opportunity to reposition
chromosomes (Heslop-Harrison and Bennett, 1990) and to
reorganise looped chromatin domains (Franke, 1974;
Franke et al., 1981; Hochstrasser et al., 1986), which may
in turn control the use of subsets of genes. Because of the
position that it occupies, its dynamics during mitosis and
the fact that it is an essential component of proliferating
cells, the lamina has been assigned a number of putative
roles both in nuclear metabolism and in nuclear envelope
assembly (Burke and Gerace, 1986; Nigg, 1989). However,
to date there is little clear cut evidence that satisfactorily
explains the function of the lamina in relation to its
structure. In this Commentary we will describe some of the
recent work that addresses this problem and attempt to
provide a unified model for the role of lamins in nuclear
envelope assembly and for the lamina in the initiation of
DNA replication