A protein-protein interaction map of the Caenorhabditis elegans 26S proteasome

被引:143
作者
Davy, A
Bello, P
Thierry-Mieg, N
Vaglio, P
Hitti, J
Doucette-Stamm, L
Thierry-Mieg, D
Reboul, J
Boulton, S
Walhout, AJM
Coux, O
Vidal, M
机构
[1] Harvard Univ, Sch Med, Dana Farber Canc Inst, Boston, MA 02115 USA
[2] Harvard Univ, Sch Med, Dept Genet, Boston, MA 02115 USA
[3] CRBM, CNRS UPR 1086, IFR 24, F-34293 Montpellier, France
[4] Imag Lab Grenoble, Lab LSR, F-38041 Grenoble, France
[5] Genome Therapeut Corp, Waltham, MA 02453 USA
[6] NIH, Natl Lib Med, Natl Ctr Biotechnol Informat, Bethesda, MD 20894 USA
关键词
D O I
10.1093/embo-reports/kve184
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 ubiquitin-proteasome proteolytic pathway is pivotal in most biological processes. Despite a great level of information available for the eukaryotic 26S proteasome-the protease responsible for the degradation of ubiquitylated proteins-several structural and functional questions remain unanswered. To gain more insight into the assembly and function of the metazoan 26S proteasome, a two-hybrid-based protein interaction map was generated using 30 Caenorhabditis elegans proteasome subunits. The results recapitulate interactions reported for other organisms and reveal new potential interactions both within the 19S regulatory complex and between the 19S and 20S subcomplexes. Moreover, novel potential proteasome interactors were identified, including an E3 ubiquitin ligase, transcription factors, chaperone proteins and other proteins not yet functionally annotated. By providing a wealth of novel biological hypotheses, this interaction map constitutes a framework for further analysis of the ubiquitin-proteasome pathway in a multicellular organism amenable to both classical genetics and functional genomics.
引用
收藏
页码:821 / 828
页数:8
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