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Nuclear matrix as an anchor for protein kinase CK2 nuclear signalling
Author(s) -
Tawfic Sherif,
Faust Russell A.,
Gapany Markus,
Ahmed Khalil
Publication year - 1996
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(199608)62:2<165::aid-jcb4>3.0.co;2-q
Subject(s) - nuclear matrix , microbiology and biotechnology , chromatin , signalling , nuclear protein , phosphorylation , protein kinase a , kinase , transcription factor , biology , chemistry , biochemistry , biophysics , gene
Nuclear matrix (NM) is not only the structural basis for nuclear shape but also is intimately involved in nuclear functional activities. Among the modulatory factors that may affect these diverse activities are the signals that may influence the state or composition of the NM proteins. One such mechanism for altering the functional activity of at least some NM proteins may be the extent of their phosphorylation. Protein kinase CK2 appears to associate with NM and to phosphorylate a number of NM‐associated proteins. Chromatin‐ and NM‐associated CK2 is rapidly modulated by mitogenic signals. We propose that NM serves as a physiological anchor for nuclear signalling of protein kinase CK2 which may influence functions of NM such as transcription of active genes and growth. © 1996 Wiley‐Liss, Inc. This article is a U.S. Government work and, as such, is in the public domain in the United States of America.