The nuclear lamina is a filamentous structure, composed of lamins, that sup
ports the inner nuclear membrane. Several integral membrane proteins includ
ing LBR (lamin B receptor), LAP (lamin-associated polypeptide) 1, and LAP 2
bind nuclear lamins in vitro and may influence lamin function and dynamics
in vivo. Results from various studies suggest that lamins may have major f
unctions in DNA replication, nuclear-envelope assembly, and nuclear-envelop
e growth. Here we discuss experimental evidence that supports these hypothe
ses and consider how interactions between lamins and other nuclear-envelope
proteins, in particular LBR and LAP2 isoforms, may contribute to or altern
atively mediate these functions of the lamina.