Chemical Inducers of Targeted Protein Degradation

被引：58

作者：

Raina, Kanak ^{[1
]}

Crews, Craig M. ^{[1
,2
,3
]}

机构：

[1] Yale Univ, Dept Chem, New Haven, CT 06520 USA

[2] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA

[3] Yale Univ, Dept Pharmacol, New Haven, CT 06520 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2010年 / 285卷 / 15期

关键词：

GENE-EXPRESSION; LIVING CELLS; UBIQUITINATION; SYSTEM; MICE; PROTEOLYSIS; PROTEASOME; MOLECULES; DIMERIZATION; MECHANISMS;

D O I：

10.1074/jbc.R109.078105

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 functions of many cellular proteins have been elucidated by selective gene inactivation and subsequent phenotypic analysis. For example, genetic mutations, gene knockout generation, and the use of RNA interference to target mRNA for degradation can all result in decreased production of a specific protein, yielding informative cellular phenotypes. However, these techniques each have certain inherent limitations. This minireview focuses on the recent development of new approaches to study protein function at the post-translational level, namely chemical induction of targeted protein degradation.

引用

收藏

页码：11057 / 11060

页数：4

相关论文

共 29 条

[1] High precision multi-genome scale reannotation of enzyme function by EFICAz [J].

Arakaki, Adrian K. ;

Tian, Weidong ;

Skolnick, Jeffrey .

BMC GENOMICS, 2006, 7 (1)

[2] Chemical control of protein stability and function in living mice [J].

Banaszynski, Laura A. ;

Sellmyer, Mark A. ;

Contag, Christopher H. ;

Wandless, Thomas J. ;

Thorne, Steve H. .

NATURE MEDICINE, 2008, 14 (10) :1123-1127

[3] A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules [J].

Banaszynski, Laura A. ;

Chen, Lin-chun ;

Maynard-Smith, Lystranne A. ;

Ooi, A. G. Lisa ;

Wandless, Thomas J. .

CELL, 2006, 126 (05) :995-1004

[4] Regulatory functions of ubiquitination in the immune system [J].

Ben-Neriah, Y .

NATURE IMMUNOLOGY, 2002, 3 (01) :20-26

[5] Recent progress with FKBP-derived destabilizing domains [J].

Chu, Bernard W. ;

Banaszynski, Laura A. ;

Chen, Ling-chun ;

Wandless, Thomas J. .

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 2008, 18 (22) :5941-5944

[6] Rapid control of protein level in the apicomplexan Toxoplasma gondii [J].

Herm-Goetz, Angelika ;

Agop-Nersesian, Carolina ;

Muenter, Sylvia ;

Grimley, Joshua S. ;

Wandless, Thomas J. ;

Frischknecht, Friedrich ;

Meissner, Markus .

NATURE METHODS, 2007, 4 (12) :1003-U8

[7] Structural basis for the recognition of hydroxyproline in αIF-1α by pVHL [J].

Hon, WC ;

Wilson, MI ;

Harlos, K ;

Claridge, TDW ;

Schofield, CJ ;

Pugh, CW ;

Maxwell, PH ;

Ratcliffe, PJ ;

Stuart, DI ;

Jones, EY .

NATURE, 2002, 417 (6892) :975-978

[8] Expression profiling reveals off-target gene regulation by RNAi [J].

Jackson, AL ;

Bartz, SR ;

Schelter, J ;

Kobayashi, SV ;

Burchard, J ;

Mao, M ;

Li, B ;

Cavet, G ;

Linsley, PS .

NATURE BIOTECHNOLOGY, 2003, 21 (06) :635-637

[9] Localization to the proteasome is sufficient for degradation [J].

Janse, DM ;

Crosas, B ;

Finley, D ;

Church, GM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (20) :21415-21420

[10] METHOTREXATE INHIBITS PROTEOLYSIS OF DIHYDROFOLATE-REDUCTASE BY THE N-END RULE PATHWAY [J].

JOHNSTON, JA ;

JOHNSON, ES ;

WALLER, PRH ;

VARSHAVSKY, A .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (14) :8172-8178