Role of A-type lamins in signaling, transcription, and chromatin organization

被引:226
作者
Andres, Vicente [1 ,2 ]
Gonzalez, Jose M. [2 ]
机构
[1] Fdn Ctr Nacl Invest Cardiovasc Carlos III, Dept Atherothrombosis & Cardiovasc Imaging, Lab Mol & Genet Cardiovasc Pathophysiol, Madrid 28029, Spain
[2] CSIC, Inst Biomed, Dept Mol & Cellular Pathol & Therapy, Lab Vasc Biol, Valencia 46010, Spain
关键词
DREIFUSS MUSCULAR-DYSTROPHY; NUCLEAR-MEMBRANE PROTEIN; DISTINCT FUNCTIONAL DOMAINS; RETINOBLASTOMA GENE-PRODUCT; TO-AUTOINTEGRATION FACTOR; POLYCOMB GROUP PROTEINS; EMERIN IN-VITRO; GERM-CELL-LESS; C-FOS; BINDING-PROTEIN;
D O I
10.1083/jcb.200904124
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
A-type lamins (lamins A and C), encoded by the LMNA gene, are major protein constituents of the mammalian nuclear lamina, a complex structure that acts as a scaffold for protein complexes that regulate nuclear structure and functions. Interest in these proteins has increased in recent years with the discovery that LMNA mutations cause a variety of human diseases termed laminopathies, including progeroid syndromes and disorders that primarily affect striated muscle, adipose, bone, and neuronal tissues. In this review, we discuss recent research supporting the concept that lamin A/C and associated nuclear envelope proteins regulate gene expression in health and disease through interplay with signal transduction pathways, transcription factors, and chromatin-associated proteins.
引用
收藏
页码:945 / 957
页数:13
相关论文
共 123 条
[1]   Mesenchymal stem cells and the artery wall [J].
Abedin, M ;
Tintut, Y ;
Demer, LL .
CIRCULATION RESEARCH, 2004, 95 (07) :671-676
[2]   Myogenin expression, cell cycle withdrawal, and phenotypic differentiation are temporally separable events that precede cell fusion upon myogenesis [J].
Andres, V ;
Walsh, K .
JOURNAL OF CELL BIOLOGY, 1996, 132 (04) :657-666
[3]   Human and mouse MOK2 proteins are associated with nuclear ribonucleoprotein components and bind specifically to RNA and DNA through their zinc finger domains [J].
Arranz, V ;
Harper, F ;
Florentin, Y ;
Puvion, E ;
Kress, M ;
ErnoultLange, M .
MOLECULAR AND CELLULAR BIOLOGY, 1997, 17 (04) :2116-2126
[4]   Nuclear envelope dystrophies show a transcriptional fingerprint suggesting disruption of Rb-MyoD pathways in muscle regeneration [J].
Bakay, M ;
Wang, ZY ;
Melcon, G ;
Schiltz, L ;
Xuan, JH ;
Zhao, P ;
Sartorelli, V ;
Seo, J ;
Pegoraro, E ;
Angelini, C ;
Shneiderman, B ;
Escolar, D ;
Chen, YW ;
Winokur, ST ;
Pachman, LM ;
Fan, CG ;
Mandler, R ;
Nevo, Y ;
Gordon, E ;
Zhu, YT ;
Dong, YB ;
Wang, Y ;
Hoffman, EP .
BRAIN, 2006, 129 :996-1013
[5]   Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo [J].
Bengtsson, L ;
Wilson, KL .
MOLECULAR BIOLOGY OF THE CELL, 2006, 17 (03) :1154-1163
[6]   Multiple and surprising new functions for emerin, a nuclear membrane protein [J].
Bengtsson, L ;
Wilson, KL .
CURRENT OPINION IN CELL BIOLOGY, 2004, 16 (01) :73-79
[7]   What MAN1 does to the smads -: TGFβ/BMP signaling and the nuclear envelope [J].
Bengtsson, Luiza .
FEBS JOURNAL, 2007, 274 (06) :1374-1382
[8]   Notch signalling: a simple pathway becomes complex [J].
Bray, Sarah J. .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2006, 7 (09) :678-689
[9]   Retinoblastoma protein recruits histone deacetylase to repress transcription [J].
Brehm, A ;
Miska, EA ;
McCance, DJ ;
Reid, JL ;
Bannister, AJ ;
Kouzarides, T .
NATURE, 1998, 391 (6667) :597-601
[10]   General transcription factors bind promoters repressed by Polycomb group proteins [J].
Breiling, A ;
Turner, BM ;
Bianchi, ME ;
Orlando, V .
NATURE, 2001, 412 (6847) :651-655