The versatile role of MSKs in transcriptional regulation

被引:115
作者
Vermeulen, Linda [1 ]
Vanden Berghe, Wim [1 ]
Beck, Ilse M. E. [1 ]
De Bosscher, Karolien [1 ]
Haegeman, Guy [1 ]
机构
[1] Univ Ghent, Dept Physiol, LEGEST, B-9000 Ghent, Belgium
关键词
NF-KAPPA-B; STRESS-ACTIVATED PROTEIN-KINASE-1; ELEMENT-BINDING PROTEIN; HISTONE H3 PHOSPHORYLATION; S6; KINASE-B; SIGNAL-TRANSDUCTION; GENE-EXPRESSION; C-FOS; MITOGEN; MEDIATE;
D O I
10.1016/j.tibs.2009.02.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Among the mitogen-activated protein kinase (MAPK) targets, MSKs (mitogen- and stress-activated protein kinases) comprise a particularly interesting protein family. Because MSKs can be activated by both extracellular-signal-regulated kinase and p38 MAPKs, they are activated by many physiological and pathological stimuli. About ten years after their original discovery, they have been recognized as versatile kinases regulating gene transcription at multiple levels. MSKs directly target transcription factors, such as cAMP-response-element-binding protein and nuclear factor-kappa B, thereby enhancing their transcriptional activity. They also induce histone phosphorylation, which is accompanied by chromatin relaxation and facilitated binding of additional regulatory proteins. Here, we review the current knowledge on MSK activation and its molecular targets, focusing on recent insights into the role of MSKs at multiple levels of transcriptional regulation.
引用
收藏
页码:311 / 318
页数:8
相关论文
共 77 条
[11]   Light stimulates MSK1 activation in the suprachiasmatic nucleus via a PACAP-ERK/MAP kinase-dependent mechanism [J].
Butcher, GQ ;
Lee, B ;
Cheng, HYM ;
Obrietan, K .
JOURNAL OF NEUROSCIENCE, 2005, 25 (22) :5305-5313
[12]   NF-κB RelA phosphorylation regulates RelA acetylation [J].
Chen, LF ;
Williams, SA ;
Mu, YJ ;
Nakano, H ;
Duerr, JM ;
Buckbinder, L ;
Greene, WC .
MOLECULAR AND CELLULAR BIOLOGY, 2005, 25 (18) :7966-7975
[13]   Loss of ATAC-specific acetylation of histone H4 at Lys12 reduces binding of JIL-1 to chromatin and phosphorylation of histone H3 at Ser10 [J].
Ciurciu, Anita ;
Komonyi, Orban ;
Boros, Imre M. .
JOURNAL OF CELL SCIENCE, 2008, 121 (20) :3366-3372
[14]   Contrasting roles of neuronal Msk1 and Rsk2 in Bad phosphorylation and feedback regulation of Erk signalling [J].
Clark, C. J. ;
McDade, D. M. ;
O'Shaughnessy, T. ;
Morris, B. J. .
JOURNAL OF NEUROCHEMISTRY, 2007, 102 (04) :1024-1034
[15]  
Davie James R, 2003, Sci STKE, V2003, pPE33
[16]   Specificity and mechanism of action of some commonly used protein kinase inhibitors [J].
Davies, SP ;
Reddy, H ;
Caivano, M ;
Cohen, P .
BIOCHEMICAL JOURNAL, 2000, 351 (351) :95-105
[17]   Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene [J].
De Cesare, D ;
Jacquot, S ;
Hanauer, A ;
Sassone-Corsi, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (21) :12202-12207
[18]   The Ets transcription factors of the PEA3 group: Transcriptional regulators in metastasis [J].
de Launoit, Yvan ;
Baert, Jean-Luc ;
Chotteau-Lelievre, Anne ;
Monte, Didier ;
Coutte, Laurent ;
Mauen, Sebastien ;
Firlej, Virginie ;
Degerny, Cindy ;
Verrernan, Kathye .
BIOCHIMICA ET BIOPHYSICA ACTA-REVIEWS ON CANCER, 2006, 1766 (01) :79-87
[19]   Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB [J].
Deak, M ;
Clifton, AD ;
Lucocq, JM ;
Alessi, DR .
EMBO JOURNAL, 1998, 17 (15) :4426-4441
[20]   Mitogen- and stress-activated protein kinase 1 activity and histone H3 phosphorylation in oncogene-transformed mouse fibroblasts [J].
Drobic, B ;
Espino, PS ;
Davie, JR .
CANCER RESEARCH, 2004, 64 (24) :9076-9079