SUMOylation is a post-translational modification that is involved in the regulation of proteins of different cellular processes. Dependent on the transient, small SUMOylated portion of most target proteins, it is difficult to identify and characterize this modification and its functions, and it is even more difficult to study the interplay between SUMOylation and other modifications on a specific protein. To facilitate the analysis of protein SUMOylation and its interplay with other protein modifications, the UFDS (Ubc9 fusion-directed SUMOylation) system has been developed. The identification of new SUMOylation substrates and the elucidation of the interplay between STAT1 (signal transducer and activator of transcription 1) phosphorylation and SUMOylation demonstrate UFDS as a useful tool for analysing protein SUMOylation.
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December 2007
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Conference Article|
November 23 2007
Ubc9 fusion-directed SUMOylation (UFDS)
R. Niedenthal
R. Niedenthal
1
1Institut für Physiologische Chemie, Medizinische Hochschule Hannover, Carl-Neuberg Strasse 1, 30625 Hannover, Germany
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Publisher: Portland Press Ltd
Received:
June 21 2007
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2007 Biochemical Society
2007
Biochem Soc Trans (2007) 35 (6): 1430–1432.
Article history
Received:
June 21 2007
Citation
R. Niedenthal; Ubc9 fusion-directed SUMOylation (UFDS). Biochem Soc Trans 1 December 2007; 35 (6): 1430–1432. doi: https://doi.org/10.1042/BST0351430
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