Nuclear matrix (NM) is not only the structural basis for nuclear shape
but also is intimately involved in nuclear functional activities. Amo
ng the modulatory factors that may affect these diverse activities are
the signals that may influence the state or composition of the NM pro
teins. One such mechanism for altering the functional activity of at l
east some NM proteins may be the extent of their phosphorylation. Prot
ein kinase CK2 appears to associate with NM and to phosphorylate a num
ber of NM-associated proteins. Chromatin- and NM-associated CK2 is rap
idly modulated by mitogenic signals. We propose that NM serves as a ph
ysiological anchor for nuclear signalling of protein kinase CK2 which
may influence functions of NM such as transcription of active genes an
d growth. (C) 1996 Wiley-Liss, Inc.