The nuclear matrix is an integral part of nuclear structure which unde
rgoes a profound reorganization during the cell cycle reflecting major
changes in functional requirements. This includes the processes of DN
A replication and gene expression at interphase and partitioning of th
e nuclear contents during mitosis. Using a monoclonal antibody (mAb2A)
which specifically stains a novel nuclear meshwork which reorganizes
during the cell cycle in Drosophila, we have initiated a study to: 1)
more closely analyze this structural reorganization; 2) clone and char
acterize the antigens recognized by this antibody; and 3) isolate othe
r interacting proteins in order to gain insight into the regulation of
this process. The mAb2A-labeled structure changes from what appears a
s a diffuse meshwork at interphase to a distinct spindle-like scaffold
at prophase. Since at metaphase the microtubules of the mitotic appar
atus co-localize with the mAb2A spindle structure, a model is consider
ed whereby the nuclear mAb2A-labeled scaffolding reorganizes during th
e cell cycle to provide a guide for the establishment of the mitotic a
pparatus. The mAb2A has identified two separate antigens, each of whic
h shows similar distribution patterns. One of these antigens has been
partially cloned and contains an unusual tandem ser-thr kinase domain.
The association of this kinase homologue with a nuclear scaffold whic
h reorganizes during the cell cycle suggests that it may be involved i
n regulating changes in nuclear architecture during the cell cycle and
/or in mediating the downstream consequences of such changes. (C) 1996
Wiley-Liss, Inc.