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Mapping the SUMO ylated landscape
Author(s) -
Eifler Karolin,
Vertegaal Alfred C.O.
Publication year - 2015
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13378
Subject(s) - sumo protein , proteome , computational biology , sumo enzymes , ubiquitin , biology , posttranslational modification , microbiology and biotechnology , proteomics , chemistry , bioinformatics , biochemistry , enzyme , gene
SUMO ylation is a post‐translational modification that regulates a multitude of cellular processes, including replication, cell‐cycle progression, protein transport and the DNA damage response. Similar to ubiquitin, SUMO (small ubiquitin‐like modifier) is covalently attached to target proteins in a reversible process via an enzymatic cascade. SUMO ylation is essential for nearly all eukaryotic organisms, and deregulation of the SUMO system is associated with human diseases such as cancer and neurodegenerative diseases. Therefore, it is of great interest to understand the regulation and dynamics of this post‐translational modification. Within the last decade, mass spectrometry analyses of SUMO proteomes have overcome several obstacles, greatly expanding the number of known SUMO target proteins. In this review, we briefly outline the basic concepts of the SUMO system, and discuss the potential of proteomic approaches to decipher SUMO ylation patterns in order to understand the role of SUMO in health and disease.