Components and regulation of nuclear transport processes

被引:197
作者
Cautain, Bastien [1 ]
Hill, Richard [2 ,3 ]
de Pedro, Nuria [1 ]
Link, Wolfgang [2 ,3 ]
机构
[1] Fdn MEDINA Parque Tecnol Ciencias Salud, Granada, Spain
[2] Univ Algarve, Dept Ciencias Biomed & Med, Regenerat Med Program, P-8005139 Faro, Portugal
[3] Univ Algarve, IBB, Ctr Biomed Mol & Estrutural, P-8005139 Faro, Portugal
关键词
anti-cancer therapy; anti-viral therapy; karyopherins; nuclear export; nuclear import; nuclear pore complex; nuclear trafficking; NF-KAPPA-B; MESSENGER-RNA EXPORT; PHENYLALANINE-GLYCINE NUCLEOPORINS; PORE COMPLEX COMPOSITION; RAN-BINDING PROTEIN-1; REV ACTIVATION DOMAIN; AMINO-ACID-SEQUENCE; LARGE-T-ANTIGEN; NUCLEOCYTOPLASMIC TRANSPORT; IMPORTIN-ALPHA;
D O I
10.1111/febs.13163
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
The spatial separation of DNA replication and gene transcription in the nucleus and protein translation in the cytoplasm is a uniform principle of eukaryotic cells. This compartmentalization imposes a requirement for a transport network of macromolecules to shuttle these components in and out of the nucleus. This nucleo-cytoplasmic transport of macromolecules is critical for both cell physiology and pathology. Consequently, investigating its regulation and disease-associated alterations can reveal novel therapeutic approaches to fight human diseases, such as cancer or viral infection. The characterization of the nuclear pore complex, the identification of transport signals and transport receptors, as well as the characterization of the Ran system (providing the energy source for efficient cargo transport) has greatly facilitated our understanding of the components, mechanisms and regulation of the nucleo-cytoplasmic transport of proteins in our cells. Here we review this knowledge with a specific emphasis on the selection of disease-relevant molecular targets for potential therapeutic intervention.
引用
收藏
页码:445 / 462
页数:18
相关论文
共 203 条
[61]   Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic Reticulum/Golgi membrane [J].
Frieman, Matthew ;
Yount, Boyd ;
Heise, Mark ;
Kopecky-Bromberg, Sarah A. ;
Palese, Peter ;
Baric, Ralph S. .
JOURNAL OF VIROLOGY, 2007, 81 (18) :9812-9824
[62]   ValidNESs: a database of validated leucine-rich nuclear export signals [J].
Fu, Szu-Chin ;
Huang, Hsuan-Cheng ;
Horton, Paul ;
Juan, Hsueh-Fen .
NUCLEIC ACIDS RESEARCH, 2013, 41 (D1) :D338-D343
[63]   Prediction of leucine-rich nuclear export signal containing proteins with NESsential [J].
Fu, Szu-Chin ;
Imai, Kenichiro ;
Horton, Paul .
NUCLEIC ACIDS RESEARCH, 2011, 39 (16) :e111
[64]   Cytoplasmic localization of mitogen-activated protein kinase kinase directed by its NH2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal [J].
Fukuda, M ;
Gotoh, I ;
Gotoh, Y ;
Nishida, E .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (33) :20024-20028
[65]   CRM1 is responsible for intracellular transport mediated by the nuclear export signal [J].
Fukuda, M ;
Asano, S ;
Nakamura, T ;
Adachi, M ;
Yoshida, M ;
Yanagida, M ;
Nishida, E .
NATURE, 1997, 390 (6657) :308-311
[66]   Nuclear export of 60S ribosomal subunits depends on Xpo1p and requires a nuclear export sequence-containing factor, Nmd3p that associates with the large subunit protein Rpl10p [J].
Gadal, O ;
Strauss, D ;
Kessl, J ;
Trumpower, B ;
Tollervey, D ;
Hurt, E .
MOLECULAR AND CELLULAR BIOLOGY, 2001, 21 (10) :3405-3415
[67]   Rhinovirus 3C Protease Can Localize in the Nucleus and Alter Active and Passive Nucleocytoplasmic Transport [J].
Ghildyal, Reena ;
Jordan, Benjamin ;
Li, Dongsheng ;
Dagher, Hayat ;
Bardin, Phillip G. ;
Gern, James E. ;
Jans, David A. .
JOURNAL OF VIROLOGY, 2009, 83 (14) :7349-7352
[68]   Importin α:: a multipurpose nuclear-transport receptor [J].
Goldfarb, DS ;
Corbett, AH ;
Mason, DA ;
Harreman, MT ;
Adam, SA .
TRENDS IN CELL BIOLOGY, 2004, 14 (09) :505-514
[69]   Exportin 4 mediates a novel nuclear import pathway for Sox family transcription factors [J].
Gontan, Cristina ;
Guettler, Thomas ;
Engelen, Erik ;
Demmers, Jeroen ;
Fornerod, Maarten ;
Grosveld, Frank G. ;
Tibboel, Dick ;
Goerlich, Dirk ;
Poot, Raymond A. ;
Rottier, Robbert J. .
JOURNAL OF CELL BIOLOGY, 2009, 185 (01) :27-34
[70]   A novel class of RanGTP binding proteins [J].
Gorlich, D ;
Dabrowski, M ;
Bischoff, FR ;
Kutay, U ;
Bork, P ;
Hartmann, E ;
Prehn, S ;
Izaurralde, E .
JOURNAL OF CELL BIOLOGY, 1997, 138 (01) :65-80