The DDR (DNA damage response) is a signalling transduction cascade utilizing many forms of post-translation modification of proteins, including phosphorylation and ubiquitination. The well-known function of ubiquitination is to target proteins for proteasomal degradation; however, it is also involved in the regulation of protein function. The present review describes how ubiquitination regulates the function of certain proteins involved in DDR, in particular FANCD2 (Fanconi's anaemia complementation group D2) and PCNA (proliferating-cell nuclear antigen). Also, the proteomic methods currently used to identify new ubiquitinated proteins in response to DNA damage, including the advantages of using the UBD (ubiquitin-binding domain) beads to purify the ubiquitinated proteins, are considered.
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February 2010
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Conference Article|
January 19 2010
Role of ubiquitination in the DNA damage response: proteomic analysis to identify new DNA-damage-induced ubiquitinated proteins
Jogitha Selvarajah;
Jogitha Selvarajah
1DNA Damage Response Group, Basic Medical Science, St George's University of London, Cranmer Terrace, Tooting, London SW17 0RE, U.K.
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Abdeladim Moumen
Abdeladim Moumen
1
1DNA Damage Response Group, Basic Medical Science, St George's University of London, Cranmer Terrace, Tooting, London SW17 0RE, U.K.
1To whom correspondence should be addressed (email amoumen@sgul.ac.uk).
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Publisher: Portland Press Ltd
Received:
May 26 2009
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2010 Biochemical Society
2010
Biochem Soc Trans (2010) 38 (1): 87–91.
Article history
Received:
May 26 2009
Citation
Jogitha Selvarajah, Abdeladim Moumen; Role of ubiquitination in the DNA damage response: proteomic analysis to identify new DNA-damage-induced ubiquitinated proteins. Biochem Soc Trans 1 February 2010; 38 (1): 87–91. doi: https://doi.org/10.1042/BST0380087
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