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SUMO2/3 is associated with ubiquitinated protein aggregates in the mouse neocortex after middle cerebral artery occlusion.

TitleSUMO2/3 is associated with ubiquitinated protein aggregates in the mouse neocortex after middle cerebral artery occlusion.
Publication TypeJournal Article
Year of Publication2015
AuthorsHochrainer K, Jackman K, Benakis C, Anrather J, Iadecola C
JournalJ Cereb Blood Flow Metab
Volume35
Issue1
Pagination1-5
Date Published2015 Jan
ISSN1559-7016
KeywordsAnimals, Blotting, Western, Disease Models, Animal, Electrophoresis, Polyacrylamide Gel, Immunoprecipitation, Infarction, Middle Cerebral Artery, Male, Mice, Inbred C57BL, Neocortex, Protein Aggregates, Reperfusion Injury, Small Ubiquitin-Related Modifier Proteins, SUMO-1 Protein, Sumoylation, Ubiquitin
Abstract

Protein modifications cooperatively act to protect the proteome from cellular stress. Focal cerebral ischemia increases protein ubiquitination, resulting in formation of ubiquitin-rich aggregates. A concurrent elevation in small ubiquitin-related modifier (SUMO)-conjugated proteins has also been reported, but a potential connection to ubiquitin remains unexplored. Here we show that SUMO2/3 conjugates are present in postischemic ubiquitin-rich aggregates, physically associated with ubiquitin. The coaggregation of SUMO2/3 and ubiquitin is induced rapidly after ischemia, depends on reperfusion, and is also observed in the absence of ischemic damage. The association between SUMO and ubiquitin suggests overlapping functional roles after ischemia/reperfusion.

DOI10.1038/jcbfm.2014.180
Alternate JournalJ. Cereb. Blood Flow Metab.
PubMed ID25352045
PubMed Central IDPMC4294403
Grant ListR01 NS034179 / NS / NINDS NIH HHS / United States
R37 NS034179 / NS / NINDS NIH HHS / United States
R37-NS34179 / NS / NINDS NIH HHS / United States