Nuclear matrix and protein kinase CK2 signaling

被引:39
作者
Ahmed, K
机构
[1] Univ Minnesota, Dept Lab Med & Pathol, Cellular & Mol Biochem Res Lab 151, Minneapolis, MN 55417 USA
[2] Dept Vet Affairs Med Ctr, Minneapolis, MN 55417 USA
来源
CRITICAL REVIEWS IN EUKARYOTIC GENE EXPRESSION | 1999年 / 9卷 / 3-4期
关键词
nuclear matrix; protein kinase CK2; signaling; nucleosome; growth stimuli; transcription;
D O I
10.1615/CritRevEukarGeneExpr.v9.i3-4.170
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The dynamic functional nature of the nuclear matrix dictates that it provide a locus for molecules involved in nuclear transduction of signals, such as those participating in cell growth control. Protein kinases are key elements in a variety of signaling mechanisms and certain of these enzymes have been shown to associate with the NM. Among these, the protein ser/thr kinase CK2 has attracted considerable attention because of its involvement in cell growth. NM appears to be a preferential locus for CK2, as evidenced from its rapid modulation in the NM in response to hormonal and growth factor signals. Differential regulation of CK2 is also noted in the transcriptionally active and inactive nucleosomes. A number of potential substrates for CK2 are localized to the NM. Likewise, distinct substrates for CK2 are noted in the transcriptionally active compared with inactive nucleosomes. The dynamics of phosphorylation of these substrates and that of the association of CK2 activity to these fractions suggests that CK2 may play a role in the functional activities of NM and provide a link between the NM and nucleosomes by serving as a factor in promoting the transition of inactive to active nucleosome.
引用
收藏
页码:329 / 336
页数:8
相关论文
共 41 条
[1]   ASSOCIATION OF CASEIN KINASE-2 WITH NUCLEAR CHROMATIN IN RELATION TO ANDROGENIC REGULATION OF RAT PROSTATE [J].
AHMED, K ;
YENICE, S ;
DAVIS, A ;
GOUELI, SA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (10) :4426-4430
[2]  
AHMED K, 1994, CELL MOL BIOL RES, V40, P1
[3]   Casein kinase II-mediated phosphorylation of the C terminus of spl decreases its DNA binding activity [J].
Armstrong, SA ;
Barry, DA ;
Leggett, RW ;
Mueller, CR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (21) :13489-13495
[4]  
Barrett TJ, 1999, VITAM HORM, V55, P127
[5]  
Berezney R, 1998, J CELL BIOCHEM, P238
[6]   Activation of nuclear transcription factor NF-κB by interleukin-1 is accompanied by casein kinase II-mediated phosphorylation of the p65 subunit [J].
Bird, TA ;
Schooley, K ;
Dower, SK ;
Hagen, H ;
Virca, GD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (51) :32606-32612
[7]  
BOUSSET K, 1993, ONCOGENE, V8, P3211
[8]  
Egyházi E, 1999, MOL CELL BIOCHEM, V191, P149
[9]   ASSOCIATION OF ELEVATED PROTEIN-KINASE CK2 ACTIVITY WITH AGGRESSIVE-BEHAVIOR OF SQUAMOUS-CELL CARCINOMA OF THE HEAD AND NECK [J].
GAPANY, M ;
FAUST, RA ;
TAWFIC, S ;
DAVIS, A ;
ADAMS, GL ;
AHMED, K .
MOLECULAR MEDICINE, 1995, 1 (06) :659-666
[10]   NUCLEAR-STRUCTURE AND THE 3-DIMENSIONAL ORGANIZATION OF DNA [J].
GETZENBERG, RH ;
PIENTA, KJ ;
WARD, WS ;
COFFEY, DS .
JOURNAL OF CELLULAR BIOCHEMISTRY, 1991, 47 (04) :289-299