@article{7ff77984df9745838fe7e491688c1543,
title = "Assay methods for small ubiquitin-like modifier (SUMO)-SUMO-interacting motif (SIM) interactions in vivo and in vitro using a split-luciferase complementation system",
abstract = "SUMOylation is a posttranslational process that attaches a small ubiquitin-like modifier (SUMO) to its target proteins covalently. SUMOylation controls multiple cellular processes through the recognition of SUMO by a SUMO-interacting motif (SIM). In this study, we developed assay systems for detecting noncovalent interactions between SUMO and SIM in cells using split-luciferase complementation. We applied a version of this assay to the detection of in vitro SUMO-SIM interactions using a bacterial expression system. These novel assays enable screening of inhibitors of SUMO-dependent protein-protein interactions, either in vivo or in vitro, in a high-throughput manner.",
keywords = "Assay, Protein-protein interactions, SIM, SUMOylation",
author = "Mikako Hirohama and Voet, {Arnout R.D.} and Takeaki Ozawa and Hisato Saitoh and Yoichi Nakao and Zhang, {Kam Y.J.} and Akihiro Ito and Minoru Yoshida",
note = "Funding Information: This work was supported in part by the Chemical Genomics Research Project, RIKEN Center for Sustainable Resource Science , RIKEN Initiative Research Unit program; a JSPS postdoctoral fellowship ; the CREST Research Project; the Japan Science and Technology Corporation ; and by Grants-in-Aid for Scientific Research (C) and for Innovative Area “Cancer” from the Ministry of Education, Culture, Sports, Science, and Technology of Japan . We thank Prof. Jeremy Tame for proofreading and Dr. Li Sheena for critical reading of this manuscript.",
year = "2014",
month = mar,
day = "1",
doi = "10.1016/j.ab.2013.12.009",
language = "English",
volume = "448",
pages = "92--94",
journal = "Analytical Biochemistry",
issn = "0003-2697",
publisher = "Academic Press Inc.",
number = "1",
}