Ubiquitin-like proteins: new wines in new bottles

被引:418
作者
Yeh, ETH [1 ]
Gong, LM
Kamitani, T
机构
[1] Univ Texas, Hlth Sci Ctr, Div Cardiol, Sch Med, Houston, TX 77030 USA
[2] Univ Texas, Hlth Sci Ctr, Div Mol Med, Sch Med, Houston, TX 77030 USA
[3] Univ Texas, Hlth Sci Ctr, Res Ctr Cardiovasc Dis, Inst Mol Med Prevent Human Dis, Houston, TX 77030 USA
基金
美国国家卫生研究院;
关键词
cullin; NEDD8; protein modification; sentrin; SUMO; ubiquitin;
D O I
10.1016/S0378-1119(00)00139-6
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Ubiquitin is a small polypeptide that covalently modifies other cellular proteins and targets them to the proteasome for degradation. In recent years, ubiquitin-dependent proteolysis has been demonstrated to play a critical role in the regulation of many cellular processes, such as cell cycle progression, cell signaling, and immune recognition. The recent discovery of three new ubiquitin-like proteins, NEDD8, Sentrin/SUMO, and Apg12, has further broadened the horizon of this type of post-translational protein modification. This review will focus on the biology and biochemistry of the Sentrin/SUMO and NEDD8 modification pathways, which are clearly distinct from the ubiquitination pathway and have unique biological functions. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:1 / 14
页数:14
相关论文
共 124 条
[31]  
Haas AL, 1997, FASEB J, V11, P1257
[32]   Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme [J].
Hahn, SL ;
Criqui, P ;
Wasylyk, B .
ONCOGENE, 1997, 15 (12) :1489-1495
[33]   mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect [J].
Hateboer, G ;
Hijmans, EM ;
Nooij, JBD ;
Schlenker, S ;
Jentsch, S ;
Bernards, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (42) :25906-25911
[34]   The ubiquitin system [J].
Hershko, A ;
Ciechanover, A .
ANNUAL REVIEW OF BIOCHEMISTRY, 1998, 67 :425-479
[35]   Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins [J].
Hicke, L .
FASEB JOURNAL, 1997, 11 (14) :1215-1226
[36]   Covalent modification of all members of human cullin family proteins by NEDD8 [J].
Hori, T ;
Osaka, F ;
Chiba, T ;
Miyamoto, C ;
Okabayashi, K ;
Shimbara, N ;
Kato, S ;
Tanaka, K .
ONCOGENE, 1999, 18 (48) :6829-6834
[37]  
Hu G, 1999, MOL CELL BIOL, V19, P724
[38]   Characterization of the mUBC9-binding sites required for E2A protein degradation [J].
Huggins, GS ;
Chin, MT ;
Sibinga, NES ;
Lee, SL ;
Haber, E ;
Lee, ME .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (40) :28690-28696
[39]   PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1 [J].
Ishov, AM ;
Sotnikov, AG ;
Negorev, D ;
Vladimirova, OV ;
Neff, N ;
Kamitani, T ;
Yeh, ETH ;
Strauss, JF ;
Maul, GG .
JOURNAL OF CELL BIOLOGY, 1999, 147 (02) :221-233
[40]  
Jiang WD, 1996, MOL GEN GENET, V251, P153