Literature DB >> 12432270

SUMO in cancer--wrestlers wanted.

Dania Alarcon-Vargas1, Ze'ev Ronai.   

Abstract

SUMO (small ubiquitin-related modifier) represents a class of ubiquitin-like proteins that is conjugated, like ubiquitin, by a set of enzymes to cellular regulatory proteins, including oncogenes and tumor suppressor genes, that play key roles in the control of cell growth, differentiation and apoptosis. SUMO conjugation affects substrates' subcellular localization and stability as well as transcriptional activities. Given the substrates involved, protein SUMOylation would be expected to be important in the course of tumorigenesis and, accordingly, altered in human cancer. Although evidence to support this notion is still scarce, this review summarizes the current knowledge of protein sumoylation and highlights the challenges to be addressed in the context of human cancer.

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Year:  2002        PMID: 12432270     DOI: 10.4161/cbt.74

Source DB:  PubMed          Journal:  Cancer Biol Ther        ISSN: 1538-4047            Impact factor:   4.742


  20 in total

1.  Modification of the erythroid transcription factor GATA-1 by SUMO-1.

Authors:  Licio Collavin; Monica Gostissa; Fabio Avolio; Paola Secco; Antonella Ronchi; Claudio Santoro; Giannino Del Sal
Journal:  Proc Natl Acad Sci U S A       Date:  2004-06-01       Impact factor: 11.205

2.  An in vitro Förster resonance energy transfer-based high-throughput screening assay for inhibitors of protein-protein interactions in SUMOylation pathway.

Authors:  Yang Song; Jiayu Liao
Journal:  Assay Drug Dev Technol       Date:  2011-12-22       Impact factor: 1.738

3.  Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2.

Authors:  Yoko Itahana; Edward T H Yeh; Yanping Zhang
Journal:  Mol Cell Biol       Date:  2006-06       Impact factor: 4.272

4.  SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage.

Authors:  Joseph-Anthony T Tan; Yujie Sun; Jing Song; Yuan Chen; Theodore G Krontiris; Linda K Durrin
Journal:  J Biol Chem       Date:  2008-04-11       Impact factor: 5.157

5.  Identification of small ubiquitin-like modifier substrates with diverse functions using the Xenopus egg extract system.

Authors:  Li Ma; Aaron Aslanian; Huaiyu Sun; Mingji Jin; Yu Shi; John R Yates; Tony Hunter
Journal:  Mol Cell Proteomics       Date:  2014-05-05       Impact factor: 5.911

6.  LMP1-Induced Sumoylation Influences the Maintenance of Epstein-Barr Virus Latency through KAP1.

Authors:  Gretchen L Bentz; Charles Randall Moss; Christopher B Whitehurst; Cary A Moody; Joseph S Pagano
Journal:  J Virol       Date:  2015-05-06       Impact factor: 5.103

7.  Development of FRET assay into quantitative and high-throughput screening technology platforms for protein-protein interactions.

Authors:  Yang Song; Vipul Madahar; Jiayu Liao
Journal:  Ann Biomed Eng       Date:  2010-12-21       Impact factor: 3.934

Review 8.  Ubiquitin proteolytic system: focus on SUMO.

Authors:  Van G Wilson; Phillip R Heaton
Journal:  Expert Rev Proteomics       Date:  2008-02       Impact factor: 3.940

9.  Sumo-1 function is dispensable in normal mouse development.

Authors:  Fu-Ping Zhang; Laura Mikkonen; Jorma Toppari; Jorma J Palvimo; Irma Thesleff; Olli A Jänne
Journal:  Mol Cell Biol       Date:  2008-06-23       Impact factor: 4.272

10.  The small ubiquitin-like modifier (SUMO) is required for gonadal and uterine-vulval morphogenesis in Caenorhabditis elegans.

Authors:  Limor Broday; Irina Kolotuev; Christine Didier; Anindita Bhoumik; Bhagwati P Gupta; Paul W Sternberg; Benjamin Podbilewicz; Ze'ev Ronai
Journal:  Genes Dev       Date:  2004-10-01       Impact factor: 11.361

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