Intermediate filaments (IFs), together with microtubules and microfilaments
build up the cytoskeleton of most eukaryotic cells. Cytoplasmic Ifs form a
dense filament network radiating from the nucleus and extending to the pla
sma membrane. The association between the cytoplasmic and nuclear surfaces
appears to provide a continuous link important for the organisation of the
cytoplasm, for cellular communication, and possibly for the transport into
and out of the nucleus. Cytoplasmic Ifs approach the nuclear surface, thin
fibrils seem to connect the Ifs with the nuclear pore complexes and a direc
t interaction of cytoplasmic Ifs with the nuclear lamin B has been observed
by in vitro binding studies. However, none of the components that cross-li
nk Ifs to the nucleus has been unambiguously identified. Furthermore, if a
direct interaction between cytoplasmic Ifs and the nuclear lamin B occurs i
n vivo, the question of how cytoplasmic Ifs get access to the nuclear inter
ior remains to be resolved. The association of Ifs with the plasma membrane
s involves different components, some of which are cell type specific. Two
specialised complexes in epithelial cells: the desmosome and the hemidesmos
ome, serve as attachment sites for keratin filaments. Desmoplakin is consid
ered as the cross-linking component of Ifs to the desmosomal plaque, wherea
s BPAG1 (bullous pemphigoid antigen) would cross-link Ifs at the hemidesmos
omal plaque. In other cell types the modality of how Ifs are anchored to th
e plasma membrane is less well understood. It involves different components
such as the spectrin based membrane skeleton, ankyrin, myosin, plectin and
certainly many other still unravelled partners. Association between the If
s and cellular membranes plays an important role in determining cell shape
and tissue integrity. Thus, the identification and characterisation of the
components involved in these interactions will be crucial for understanding
the function of intermediate filaments.