TY - CHAP
T1 - Concepts and methodologies to study protein SUMOylation
T2 - An overview
AU - Matunis, Michael J.
AU - Rodriguez, Manuel S.
N1 - Funding Information:
This work was supported by the National Institutes of Health (GM060980 to M.J.M.). M.S.R. would like to acknowledge the Proteostasis COST action (BM1307
Publisher Copyright:
© Springer Science+Business Media New York 2016.
PY - 2016/9/1
Y1 - 2016/9/1
N2 - Protein modification by the small ubiquitin-related modifier (SUMO) was simultaneously discovered by several groups at the middle of the 1990s. Although distinct names were proposed including Sentrin, GMP1, PIC1, or SMT3, SUMO became the most popular. Early studies on the functions of SUMOylation focused on activities in the nucleus, including transcription activation, chromatin structure, and DNA repair. However, it is now recognized that SUMOylation affects a large diversity of cellular processes both in the nucleus and the cytoplasm and functions of SUMOylation appear to have undefined limits. SUMOconjugating enzymes and specific proteases actively regulate the modification status of target proteins. The recent discoveries of ubiquitin-SUMO hybrid chains, multiple SUMO-interacting motifs, and macromolecular complexes regulated by SUMOylation underscore the high complexity of this dynamic reversible system. New conceptual frameworks suggested by these findings have motivated the development of new methodologies to study pre-and post-SUMOylation events in vitro and in vivo, using distinct model organisms. Here we summarize some of the new developments and methodologies in the field, particularly those that will be further elaborated on in the chapters integrating this book.
AB - Protein modification by the small ubiquitin-related modifier (SUMO) was simultaneously discovered by several groups at the middle of the 1990s. Although distinct names were proposed including Sentrin, GMP1, PIC1, or SMT3, SUMO became the most popular. Early studies on the functions of SUMOylation focused on activities in the nucleus, including transcription activation, chromatin structure, and DNA repair. However, it is now recognized that SUMOylation affects a large diversity of cellular processes both in the nucleus and the cytoplasm and functions of SUMOylation appear to have undefined limits. SUMOconjugating enzymes and specific proteases actively regulate the modification status of target proteins. The recent discoveries of ubiquitin-SUMO hybrid chains, multiple SUMO-interacting motifs, and macromolecular complexes regulated by SUMOylation underscore the high complexity of this dynamic reversible system. New conceptual frameworks suggested by these findings have motivated the development of new methodologies to study pre-and post-SUMOylation events in vitro and in vivo, using distinct model organisms. Here we summarize some of the new developments and methodologies in the field, particularly those that will be further elaborated on in the chapters integrating this book.
KW - History
KW - Methodologies
KW - SUMOylation
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U2 - 10.1007/978-1-4939-6358-4_1
DO - 10.1007/978-1-4939-6358-4_1
M3 - Chapter
C2 - 27631794
AN - SCOPUS:84987749771
T3 - Methods in Molecular Biology
SP - 3
EP - 22
BT - Methods in Molecular Biology
PB - Humana Press Inc.
ER -