Ubiquitin-like protein modifications in prostate and breast cancer

被引:17
作者
Wu, Fangting [1 ]
Mo, Yin-Yuan [1 ]
机构
[1] So Illinois Univ, Dept Med Microbiol Immunol & Cell Biol, Springfield, IL 62794 USA
来源
FRONTIERS IN BIOSCIENCE-LANDMARK | 2007年 / 12卷
关键词
posttranslational modification; ubiquitin-like protein; sumoylation; Ubc9; prostate cancer and breast cancer;
D O I
10.2741/2094
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
Post-translational modifications by ubiquitin-like proteins have been implicated in the regulation of diverse cellular processes, including nuclear transport, transcription regulation, stress response and DNA repair. Ubiquitination is well characterized for its roles in regulating these cellular processes. As a newly identified member of ubiquitin-like proteins, the small ubiquitin-like modifier (SUMO) has received a great deal of attention for its functions distinct from ubiquitin. In particular, alterations of SUMO conjugation or sumoylation have been implicated in several human diseases, including cancer. Although little is known about the underlying mechanism of sumoylation-associated tumorigenesis, the modulation of nuclear receptor (NR)-mediated signaling pathways is likely to play a role in this aspect. NRs are a family of ligand dependent transcription factors which control cell growth and differentiation in many cell types, as well as during the development of cancer. In this review, we will discuss some basic aspects of sumoylation and how sumoylation modulates the NR-mediated gene expression, focusing on androgen receptor (AR) and estrogen receptor (ER), a key player in progression of prostate or breast cancer.
引用
收藏
页码:700 / 711
页数:12
相关论文
共 119 条
[1]   Ikaros SUMOylation: Switching out of repression [J].
Arco, PGD ;
Koipally, J ;
Georgopoulos, K .
MOLECULAR AND CELLULAR BIOLOGY, 2005, 25 (07) :2688-2697
[2]   Expression and regulation of the mammalian SUMO-1 E1 enzyme [J].
Azuma, Y ;
Tan, SH ;
Cavenagh, MM ;
Ainsztein, AM ;
Saitoh, H ;
Dasso, M .
FASEB JOURNAL, 2001, 15 (08) :1825-+
[3]   Herpes simplex virus 1 ICPO co-localizes with a SUMO-specific protease [J].
Bailey, D ;
O'Hare, P .
JOURNAL OF GENERAL VIROLOGY, 2002, 83 :2951-2964
[4]   Structure determination of the small ubiquitin-related modifier SUMO-1 [J].
Bayer, P ;
Arndt, A ;
Metzger, S ;
Mahajan, R ;
Melchior, F ;
Jaenicke, R ;
Becker, J .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 280 (02) :275-286
[5]   Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation [J].
Bencsath, KP ;
Podgorski, MS ;
Pagala, VR ;
Slaughter, CA ;
Schulman, BA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (49) :47938-47945
[6]   Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1 [J].
Bernier-Villamor, V ;
Sampson, DA ;
Matunis, MJ ;
Lima, CD .
CELL, 2002, 108 (03) :345-356
[7]   SUMO-1 protease-1 regulates gene transcription through PML [J].
Best, JL ;
Ganiatsas, S ;
Agarwal, S ;
Changou, A ;
Salomoni, P ;
Shirihai, O ;
Meluh, PB ;
Pandolfi, PP ;
Zon, LI .
MOLECULAR CELL, 2002, 10 (04) :843-855
[8]   Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity [J].
Bies, J ;
Markus, J ;
Wolff, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (11) :8999-9009
[9]   A mechanism for inhibiting the SUMO pathway [J].
Boggio, R ;
Colombo, R ;
Hay, RT ;
Draetta, GF ;
Chiocca, S .
MOLECULAR CELL, 2004, 16 (04) :549-561
[10]   The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast [J].
Bylebyl, GR ;
Belichenko, I ;
Johnson, ES .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (45) :44113-44120