The mobility of Bach2 nuclear foci is regulated by SUMO-1 modification
- Department of Cellular Biology, Research Institute for Radiation Biology and Medicine, Hiroshima University, Kasumi 1-2-3, Minamiku, Hiroshima 734-8553 (Japan)
- National Institute of Advanced Industrial Science and Technology, Research Institute for Cell Engineering, Osaka 563-8577 (Japan)
- Department of Pediatrics, Hiroshima University Graduate School of Medicine, Hiroshima 734-8553 (Japan)
- The Hospital for Sick Children, Research Institute, Toronto, ON, M5G 1L7 (Canada)
- Department of Biochemistry, Tohoku University Graduate School of Medicine, Sendai 980-8575 (Japan)
The small ubiquitin-like modifier-1 (SUMO-1) modulates the functions of nuclear proteins by changing their structure and/or subnuclear localization. Several nuclear proteins form dynamic higher order nuclear structures, termed non-chromatin nuclear domains, which are involved in the regulation of nuclear function. However, the role that SUMO modification of the component proteins plays in the regulation of the activity and function of nuclear domains is unclear. Here we demonstrate that nuclear domains formed by Bach2, a transcription repressor, show restricted movement and undergo fusion events upon oxidative stress. Mutation of the SUMO-acceptor lysines in Bach2 alters the behavior of these nuclear foci and results in a decreased frequency of fusion events. We propose that SUMO modification is an important regulatory system for the mobility of the nuclear domains formed by Bach2.
- OSTI ID:
- 21045943
- Journal Information:
- Experimental Cell Research, Vol. 314, Issue 4; Other Information: DOI: 10.1016/j.yexcr.2007.12.013; PII: S0014-4827(07)00585-X; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0014-4827
- Country of Publication:
- United States
- Language:
- English
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