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pubmed-article:18451503pubmed:abstractTextSmall ubiquitin-related modifier (SUMO) is a type I ubiquitin-like protein family member and is covalently attached to various target proteins. Through this post-translational modification, SUMO plays important roles in various cellular events. Here, we show that SUMO is secreted from cultured cells in an endoplasmic reticulum (ER)/Golgi-independent manner and that this secretion occurs without covalent binding to target proteins or chain formation. Overexpression experiments using C-terminally truncated mutants of SUMO revealed that the secretion requires the C-terminal sequence. Recombinant SUMO-3 protein was capable of binding to and promoting the proliferation of cultured cells. Thus, we propose that SUMO functions as a cytokine-like molecule extracellularly.lld:pubmed
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pubmed-article:18451503pubmed:year2008lld:pubmed
pubmed-article:18451503pubmed:articleTitleSmall ubiquitin-related modifier is secreted and shows cytokine-like activity.lld:pubmed
pubmed-article:18451503pubmed:affiliationDepartment of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.lld:pubmed
pubmed-article:18451503pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18451503pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed