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Literature DB >> 18598940

The HECT family of E3 ubiquitin ligases: multiple players in cancer development.

Francesca Bernassola¹, Michael Karin, Aaron Ciechanover, Gerry Melino.

Abstract

The involvement of the homologous to E6-AP carboxyl terminus (HECT)-type E3s in crucial signaling pathways implicated in tumorigenesis is presently an area of intense research and extensive scientific interest. This review highlights recent discoveries on the ubiquitin-mediated degradation of crucial tumor suppressor molecules catalyzed by the HECT-type E3s. By providing a portrait of their protein targets, we intend to link the substrate specificity of HECT-type E3s with their contribution to tumorigenesis. Moreover, we discuss the relevance of targeting the HECT E3s, through the development of small-molecule inhibitors, as an anticancer therapeutic strategy.

Entities: Disease Gene

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Year: 2008 PMID： 18598940 DOI： 10.1016/j.ccr.2008.06.001

Source DB: PubMed Journal: Cancer Cell ISSN： 1535-6108 Impact factor: 31.743

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Cited

263 in total

1. Human proteome-scale structural modeling of E2-E3 interactions exploiting interface motifs.

Authors: Gozde Kar; Ozlem Keskin; Ruth Nussinov; Attila Gursoy
Journal: J Proteome Res Date: 2012-01-10 Impact factor: 4.466

Review 2. Twists and turns in ubiquitin-like protein conjugation cascades.

Authors: Brenda A Schulman
Journal: Protein Sci Date: 2011-11-09 Impact factor: 6.725

3. Bul proteins, a nonredundant, antagonistic family of ubiquitin ligase regulatory proteins.

Authors: Tatiana V Novoselova; Kiran Zahira; Ruth-Sarah Rose; James A Sullivan
Journal: Eukaryot Cell Date: 2012-02-03

4. The ubiquitin E3 ligase WWP1 decreases CXCL12-mediated MDA231 breast cancer cell migration and bone metastasis.

Authors: Kristina Subik; Lei Shu; Chengyu Wu; Qianqian Liang; David Hicks; Brendan Boyce; Linda Schiffhauer; Di Chen; Ceshi Chen; Ping Tang; Lianping Xing
Journal: Bone Date: 2012-01-11 Impact factor: 4.398

5. Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination.

Authors: Zhizhi Wang; Gregory A Michaud; Zhihong Cheng; Yue Zhang; Thomas R Hinds; Erkang Fan; Feng Cong; Wenqing Xu
Journal: Genes Dev Date: 2012-01-19 Impact factor: 11.361

The HECT family of E3 ubiquitin ligases: multiple players in cancer development.

1. Human proteome-scale structural modeling of E2-E3 interactions exploiting interface motifs.

Review 2. Twists and turns in ubiquitin-like protein conjugation cascades.

3. Bul proteins, a nonredundant, antagonistic family of ubiquitin ligase regulatory proteins.

4. The ubiquitin E3 ligase WWP1 decreases CXCL12-mediated MDA231 breast cancer cell migration and bone metastasis.

5. Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination.

Review 6. The role of deubiquitinating enzymes in apoptosis.

7. Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2.

8. Characterizing WW domain interactions of tumor suppressor WWOX reveals its association with multiprotein networks.

Review 9. Targeting the ubiquitin pathway for cancer treatment.

10. miR-100 antagonism triggers apoptosis by inhibiting ubiquitination-mediated p53 degradation.